KEGG   ENZYME: 1.17.5.3
Entry
EC 1.17.5.3                 Enzyme                                 

Name
formate dehydrogenase-N;
Fdh-N;
FdnGHI;
nitrate-inducible formate dehydrogenase;
formate dehydrogenase N;
FDH-N;
nitrate inducible Fdn;
nitrate inducible formate dehydrogenase
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With a quinone or similar compound as acceptor
Sysname
formate:quinone oxidoreductase
Reaction(IUBMB)
formate + a quinone = CO2 + a quinol [RN:R09494]
Reaction(KEGG)
R09494
Substrate
formate [CPD:C00058];
quinone [CPD:C00472]
Product
CO2 [CPD:C00011];
quinol [CPD:C00530]
Comment
The enzyme contains molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters and two heme b groups. Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm. The system generates proton motive force under anaerobic conditions [3].
History
EC 1.17.5.3 created 2010 as EC 1.1.5.6, transferred 2017 to EC 1.17.5.3
Orthology
K08348  formate dehydrogenase-N, alpha subunit
Genes
ECO: b1474(fdnG)
ECJ: JW1470(fdnG)
ECD: ECDH10B_1605(fdnG)
EBW: BWG_1295(fdnG)
ECOK: ECMDS42_1186(fdnG)
ECE: Z2236(fdnG)
ECS: ECs2078
EOI: ECO111_1864(fdnG)
EOJ: ECO26_2072(fdnG)
EOH: ECO103_1603(fdnG)
ECOO: ECRM13514_1928(fdnG)
ECOH: ECRM13516_1830(fdnG)
ECK: EC55989_1605(fdnG)
ECG: E2348C_1608(fdnG)
ELH: ETEC_1545
ECW: EcE24377A_1655(fdnG)
ECV: APECO1_609(fdnG)
ECX: EcHS_A1557(fdnG)
ECM: EcSMS35_1700(fdnG)
ECR: ECIAI1_1477(fdnG)
ECQ: ECED1_1624(fdnG)
EUM: ECUMN_1727(fdnG)
ECT: ECIAI39_1736(fdnG)
EOC: CE10_1663(fdnG)
EBR: ECB_01432(fdnG)
EBL: ECD_01432(fdnG)
EBE: B21_01444(fdnG)
EBD: ECBD_2165
ECI: UTI89_C1689(fdnG)
EIH: ECOK1_1631(fdnG)
ECZ: ECS88_1566(fdnG)
ECC: c5623(fdnG)
ELO: EC042_1604(fdnG)
EAB: ECABU_c17080(fdnG)
EDJ: ECDH1ME8569_1417(fdnG)
ELW: ECW_m1602(fdnG)
ELL: WFL_07835(fdnG1)
ELP: P12B_c1654(fdnG) P12B_c1655(fdnG)
ELF: LF82_0630(fdnG)
EFE: EFER_1489(fdnG)
ESZ: FEM44_22465(fdnG)
STM: STM1570(fdnG)
SEO: STM14_1894(fdnG)
SEY: SL1344_1500(fdnG)
SEB: STM474_1583(fdnG)
SEF: UMN798_1644(fdnG) UMN798_1645(fdnG)
SENR: STMDT2_14931(fdnG)
SPT: SPA1298(fdnG)
SEK: SSPA1206
SEG: SG1557(fdnG)
SET: SEN1485(fdnG)
SENB: BN855_16160(fdnG)
SFL: SF1751(fdnG)
SFX: S1884(fdnG)
SFV: SFV_1747(fdnG)
SSN: SSON_1650(fdnG)
SBO: SBO_1583(fdnG)
ECLO: ENC_09820
EEC: EcWSU1_02353(fdnG) EcWSU1_02354(fdnG)
ECHG: FY206_12940(fdnG)
ESH: C1N69_11665(fdnG)
EBG: FAI37_17690(fdnG)
KPN: KPN_01867(fdnG)
KPU: KP1_2931(fdnG)
KPP: A79E_2378
KPR: KPR_2929(fdnG)
KPX: PMK1_04207(fdnG_1) PMK1_04208(fdnG_2)
KPNK: BN49_2967(fdnG)
KPE: KPK_2489(fdnG)
KOE: A225_2876
CRO: ROD_15621(fdnG)
CBRA: A6J81_04390(fdnG) A6J81_04780(fdnG)
CIF: AL515_12255(fdnG)
CFAR: CI104_13145(fdnG)
CIR: C2U53_22215(fdnG)
CPAR: CUC49_07970(fdnG)
CTEL: GBC03_13400(fdnG) GBC03_17345(fdnG)
RAO: DSD31_13360(fdnG)
RTG: NCTC13098_06023(fdnG_1)
REE: electrica_02598(fdnG_1) electrica_02600(fdnG_2) electrica_04112(fdnG_3)
KOR: AWR26_12790(fdnG)
KOT: EH164_11525(fdnG) EH164_11845(fdnG)
KPSE: IP581_11315(fdnG)
LEI: C2U54_16530(fdnG)
LER: GNG29_11045(fdnG)
LEA: GNG26_11310(fdnG)
AHN: NCTC12129_00262(fdnG_2) NCTC12129_03677(fdnG_3)
YRE: HEC60_05625(fdnG)
PDZ: HHA33_13540(fdnG) HHA33_15130(fdnG)
EBC: C2U52_21525(fdnG) C2U52_23225(fdnG)
IZH: FEM41_12715(fdnG)
SERA: Ser39006_010700(fdnG)
SERQ: CWC46_10695(fdnG)
RAA: Q7S_00210
RACE: JHW33_16845(fdnG)
ECA: ECA1408(fdnG)
PATR: EV46_07130
PATO: GZ59_14450(fdnG)
PCT: PC1_1286
PEC: W5S_3034
PPUJ: E2566_07135(fdnG)
DDD: Dda3937_02963(fdnG)
DFN: CVE23_08490(fdnG)
DDQ: DDI_1292
DAQ: DAQ1742_01388(fdoG) DAQ1742_01538(fdnG)
DIC: Dpoa569_002332(fdnG)
PAJ: PAJ_0232(FdnG)
PVA: Pvag_3327(fdnG)
PAGG: AL522_04785(fdnG)
PCD: C2E16_00880(fdnG)
MINT: C7M51_03641(fdnG)
MTHI: C7M52_03392(fdnG)
PAY: PAU_00744(fdnG)
PVG: CRN77_04695(fdnG)
PHAU: PH4a_06470(fdnG)
PCOL: F1325_18505(fdnG)
PCIB: F9282_19075(fdnG)
PRG: RB151_014060(fdnG_1) RB151_014070(fdnG_2)
PALA: CO695_16965(fdnG)
PHEI: NCTC12003_00220(fdnG)
PRQ: CYG50_09120(fdnG)
PVC: G3341_13440(fdnG)
HPAR: AL518_01330(fdnG)
LPV: HYN51_13205(fdnG)
PRAG: EKN56_03610(fdnG)
ADP: NCTC12871_00141(fdnG)
PMK: MDS_4225
PPRC: PFLCHA0_c32650(fdoG)
PPRO: PPC_3259
AVL: AvCA_03810(fdhA)
AVD: AvCA6_03810(fdhA)
ACX: Achr_37960(fdhA)
SON: SO_0101(fdnG)
SPL: Spea_0437
SHL: Shal_0492
NEI: BG910_02450(fdnG)
NBL: GJV52_02430(fdnG)
CNC: CNE_2c14340(fdoG)
CTI: RALTA_B1681(fdnG)
COX: E0W60_02610(fdnG)
ODI: ODI_R1009
CJU: C8J_1415
CJM: CJM1_1456(fdhA)
CJQ: UC78_1444(fdnG)
ABT: ABED_1396
GSK: KN400_0757(fdnG)
GUR: Gura_3388
GBM: Gbem_2267(fdnG-1)
GEO: Geob_1634(fdnG-1)
GEM: GM21_1955
GEB: GM18_1962
GBN: GEOBRER4_21210(fdnG)
APK: APA386B_352(fdnG)
ASZ: ASN_3403(fdoG)
APOM: CPF11_12735(fdnG)
ATO: CIW82_14445(fdnG)
ACET: DS739_07695(fdnG)
NEH: E3E11_02405(fdnG)
SWF: E3E12_02660(fdnG)
AZM: DM194_14325(fdnG)
BBEV: BBEV_0717(fdhA-1)
BDA: FSZ17_22305(fdnG)
NMK: CHR53_27385(fdnG)
AIA: AWH56_013365(fdnG)
BSE: Bsel_1218
SALQ: SYNTR_0512
 » show all
Reference
1  [PMID:1099093]
  Authors
Enoch HG, Lester RL
  Title
The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli.
  Journal
J Biol Chem 250:6693-705 (1975)
  Sequence
Reference
2  [PMID:11884747]
  Authors
Jormakka M, Tornroth S, Byrne B, Iwata S
  Title
Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
  Journal
Science 295:1863-8 (2002)
DOI:10.1126/science.1068186
  Sequence
Reference
3  [PMID:11752799]
  Authors
Jormakka M, Tornroth S, Abramson J, Byrne B, Iwata S
  Title
Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli.
  Journal
Acta Crystallogr D Biol Crystallogr 58:160-2 (2002)
DOI:10.1107/S0907444901017723
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.17.5.3
IUBMB Enzyme Nomenclature: 1.17.5.3
ExPASy - ENZYME nomenclature database: 1.17.5.3
BRENDA, the Enzyme Database: 1.17.5.3

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