KEGG   ENZYME: 1.17.99.7
Entry
EC 1.17.99.7                Enzyme                                 

Name
formate dehydrogenase (acceptor);
FDHH;
FDH-H;
FDH-O;
formate dehydrogenase H;
formate dehydrogenase O
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With unknown physiological acceptors
Sysname
formate:acceptor oxidoreductase
Reaction(IUBMB)
formate + acceptor = CO2 + reduced acceptor [RN:R09481]
Reaction(KEGG)
R09481
Substrate
formate [CPD:C00058];
acceptor [CPD:C00028]
Product
CO2 [CPD:C00011];
reduced acceptor [CPD:C00030]
Comment
Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase. The two enzymes form the formate-hydrogen lyase complex [1]. The enzyme contains an [4Fe-4S] cluster, a selenocysteine residue and a molybdopterin cofactor [1].
History
EC 1.17.99.7 created 2010 as EC 1.1.99.33, transferred 2017 to EC 1.17.99.7
Orthology
K22015  formate dehydrogenase (acceptor)
Genes
ECO: b4079(fdhF)
ECJ: JW4040(fdhF)
ECD: ECDH10B_4270(fdhF)
EBW: BWG_3793(fdhF)
ECOK: ECMDS42_3518(fdhF)
ECE: Z5678(fdhF)
ECS: ECs5061
ETW: ECSP_5176(fdhF)
EOI: ECO111_4955(fdhF)
EOJ: ECO26_5197(fdhF)
EOH: ECO103_4830(fdhF)
ECOO: ECRM13514_5289(fdhF)
ECOH: ECRM13516_4957(fdhF)
ECK: EC55989_4574(fdhF)
ECG: E2348C_4407(fdhF)
ELH: ETEC_4389
ECW: EcE24377A_4635(fdhF)
ENA: ECNA114_4260(fdhF1) ECNA114_42601(fdhF2)
ECV: APECO1_2372(fdhF) APECO1_23722(fdhF)
ECX: EcHS_A4324(fdhF)
ECM: EcSMS35_4542(fdhF)
ECR: ECIAI1_4313(fdhF)
ECQ: ECED1_4812(fdhF)
EUM: ECUMN_4615(fdhF)
ECT: ECIAI39_4501(fdhF)
EBR: ECB_03951(fdhF)
EBL: ECD_03951(fdhF)
EBE: B21_03911(fdhF)
EIH: ECOK1_4590(fdhF)
ECZ: ECS88_4577(fdhF)
ECC: c5625(fdhF)
ELO: EC042_4450(fdhF)
EKF: KO11_01960(fdhF1)
EAB: ECABU_c46300(fdhF)
EDJ: ECDH1ME8569_3937(fdhF)
ELW: ECW_m4445(fdhF)
ELL: WFL_21615(fdhF2) WFL_21620(fdhF1)
ELP: P12B_c4188(fdhF) P12B_c4189(fdhF)
ELF: LF82_0629(fdhF)
ECOI: ECOPMV1_04537(fdhF_2)
EFE: EFER_4292(fdhF)
EAL: EAKF1_ch1803(napA)
STY: STY4484(fdhF)
STT: t4192(fdhF)
STM: STM4285(fdhF)
SEO: STM14_5155(fdhF)
SEY: SL1344_4221(SC4B5.11c)
SEB: STM474_4481(fdhF)
SENR: STMDT2_41351(SC4B5.11c) STMDT2_41361
SPT: SPA4103(fdhF)
SEG: SG4130(fdhF)
SET: SEN4056(fdhF)
SENB: BN855_43600(fdhF)
SBG: SBG_3723(fdhF)
SFT: NCTC1_04501(fdhF_3) NCTC1_04503(fdhF_4)
ECLO: ENC_05080
EEC: EcWSU1_00297(fdhF) EcWSU1_00298(fdhF) EcWSU1_01854(fdhF)
ESA: ESA_02058
CTU: CTU_19050(fdhF) CTU_19090 CTU_19100(fdhF)
KPN: KPN_02090 KPN_04482(fdhF)
KPU: KP1_0346(fdhF) KP1_3178
KPJ: N559_2200
KPX: PMK1_01954(fdhF_1) PMK1_01955(fdhF_2) PMK1_04454(fdhF_4)
KPNK: BN49_3195(fdhF) BN49_4950(fdhF2)
KPE: KPK_2240(fdhA) KPK_5187(fdhF)
EAE: EAE_17440
CRO: ROD_33911(fdhF) ROD_34681(fdhF)
EBT: EBL_c29640(fdhF1) EBL_c36300(fdhF2) EBL_c36310(fdhF)
RTG: NCTC13098_03133(fdhF_2) NCTC13098_06795(fdhF_8)
REE: electrica_02153(fdhF_1) electrica_04714(fdhF_3) electrica_04716(fdhF_4)
CLAP: NCTC11466_02884(fdhF_2) NCTC11466_04247(fdhF_3) NCTC11466_04668(fdhF_4)
KIE: NCTC12125_03409(fdhF_1) NCTC12125_04990(fdhF_2)
AHN: NCTC12129_03658(fdhF_2) NCTC12129_03684(fdhF_4)
YRE: HEC60_19515(fdhF)
YPE: YPO0344(fdhF)
YPK: y0601(fdhF)
YPH: YPC_0658(fdhF)
YPA: YPA_3938
YPN: YPN_3326
YPM: YP_0498(fdhF)
YPG: YpAngola_A0729(fdhF)
YPZ: YPZ3_0346(fdhF)
YPD: YPD4_0299(fdhF)
YPX: YPD8_0300(fdhF)
YPW: CH59_1521
YPJ: CH55_3420
YPV: BZ15_3228
YPL: CH46_571
YPS: YPTB0398(fdhF)
YPO: BZ17_2171
YPI: YpsIP31758_3682(fdhF)
YPY: YPK_3829
YPB: YPTS_0424
YPQ: DJ40_2009
YPU: BZ21_3768
YPR: BZ20_1713
YPC: BZ23_4038
YPF: BZ19_3869
YEN: YE2810(fdhF)
YEY: Y11_17131
YEW: CH47_2161
YET: CH48_3062
YEE: YE5303_32391(fdhF)
YAL: AT01_3940
YRO: CH64_16
YMO: HRD69_07595(fdhF) HRD69_12780(fdhF)
SPE: Spro_2424
SRL: SOD_c40300(fdhF)
SPLY: Q5A_021925(fdhF)
RAA: Q7S_05530
ECA: ECA1250(fdhF) ECA1507
PATO: GZ59_12770(fdhF) GZ59_15440
PCT: PC1_1383
PEC: W5S_1695
DDD: Dda3937_00742(fdhF)
DDQ: DDI_1212
DAQ: DAQ1742_01476(fdhF)
MINT: C7M51_00234(fdhF_1) C7M51_00235(fdhF_2) C7M51_00238(fdhF_3) C7M51_04185(fdhF_4) C7M51_04186(fdhF_5)
MTHI: C7M52_02870(fdhF_1) C7M52_02871(fdhF_2)
PMR: PMI2979(fdhF) PMI3577(fdhF)
PMIB: BB2000_0019(fdhF) BB2000_2992(fdhF)
PHEI: NCTC12003_01142(fdhF)
PRJ: NCTC6933_03528(fdhF_2)
ANS: ArsFIN_30500(fdhF_1) ArsFIN_30510(fdhF_2)
ETR: ETAE_2900(fdhF1) ETAE_2901(fdhF2)
ETD: ETAF_2635(fdhF1) ETAF_3337
LRI: NCTC12151_03356(fdhF)
PDZ: HHA33_00260(fdhF) HHA33_07720(fdhF)
HPR: PARA_17740(fdhF) PARA_17750(fdhF)
HPIT: NCTC13334_00723(fdhF)
HHZ: NCTC10839_01330(fdhF)
PDAG: 4362423_00443(fdxG)
PAET: NCTC13378_00579(fdxG)
FES: HER31_04640(fdhF)
AHA: AHA_2495(fdhA)
ASA: ASA_1821(fdhF)
AEL: NCTC12917_01740(fdhF_1) NCTC12917_01741(fdhF_2)
ORB: IPMB12_03190(fdhF)
OFO: BRW83_2235(fdhF)
HHE: HH_0229
HCE: HCW_06570
HCM: HCD_05390
CFZ: CSG_16780
SDL: Sdel_2075
NAM: NAMH_1306
DMA: DMR_43550
DSF: UWK_00299
RPC: RPC_4578
OCA: OCAR_5289
RRU: Rru_A0324
RRF: F11_01635
ALI: AZOLI_p30033(fdhF)
PPY: PPE_02669
PPM: PPSC2_14235(fdhF)
PPO: PPM_2863(fdhF)
PPOL: X809_30625
PPOY: RE92_22465
PSAB: PSAB_11930
PRI: PRIO_3937(fdhF)
CBE: Cbei_3801
CBZ: Cbs_3801
CBEI: LF65_04285
CPAS: Clopa_0987
CPAT: CLPA_c10260(fdhF)
CPAE: CPAST_c10260(fdhF)
CDF: CD630_33170(fdhF)
PDC: CDIF630_03619(fdhF)
CDL: CDR20291_3179(fdhF)
PDF: CD630DERM_33170(fdhF)
ROC: HF520_14630(fdhF)
STH: STH3296
AWO: Awo_c08190(fdhF1) Awo_c08210(fdhF2)
MTHO: MOTHE_c22530(fdhF2)
MTHZ: MOTHA_c23260(fdhF2)
TPZ: Tph_c26250(fdhA4)
PFT: JBW_03697
STED: SPTER_13890(fdhF_2) SPTER_13900(fdhF_3)
LPIL: LIP_0597
ELE: Elen_2859
AEQ: AEQU_0303
TPI: TREPR_3099(fdhA)
MWO: MWSIV6_0093(fdhA3)
HALH: HTSR_1347
HHSR: HSR6_1419
HDF: AArcSl_2794(phsA3)
STEP: IC006_0502
 » show all
Reference
1  [PMID:2211698]
  Authors
Axley MJ, Grahame DA, Stadtman TC
  Title
Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component.
  Journal
J Biol Chem 265:18213-8 (1990)
  Sequence
[eco:b4079]
Reference
2  [PMID:8626495]
  Authors
Gladyshev VN, Boyington JC, Khangulov SV, Grahame DA, Stadtman TC, Sun PD
  Title
Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis.
  Journal
J Biol Chem 271:8095-100 (1996)
DOI:10.1074/jbc.271.14.8095
  Sequence
[eco:b4079]
Reference
3  [PMID:9521673]
  Authors
Khangulov SV, Gladyshev VN, Dismukes GC, Stadtman TC
  Title
Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.
  Journal
Biochemistry 37:3518-28 (1998)
DOI:10.1021/bi972177k
  Sequence
[eco:b4079]
Other DBs
ExplorEnz - The Enzyme Database: 1.17.99.7
IUBMB Enzyme Nomenclature: 1.17.99.7
ExPASy - ENZYME nomenclature database: 1.17.99.7
BRENDA, the Enzyme Database: 1.17.99.7

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