EC                 Enzyme                                 

formylmethanofuran dehydrogenase;
formylmethanofuran:acceptor oxidoreductase
Acting on the aldehyde or oxo group of donors;
With an iron-sulfur protein as acceptor
formylmethanofuran:ferredoxin oxidoreductase
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ [RN:R11743]
R11743 > R03015;
(other) R08060
formylmethanofuran [CPD:C01001];
H2O [CPD:C00001];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139]
CO2 [CPD:C00011];
methanofuran [CPD:C00862];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080]
Contains a molybdopterin cofactor and numerous [4Fe-4S] clusters. In some organisms an additional subunit enables the incorporation of tungsten when molybdenum availability is low. The enzyme catalyses a reversible reaction in methanogenic archaea, and is involved in methanogenesis from CO2 as well as the oxidation of coenzyme M to CO2. The reaction is endergonic, and is driven by coupling with the soluble CoB-CoM heterodisulfide reductase via electron bifurcation.
EC created 1992 as EC, transferred 2017 to EC
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
K00200  formylmethanofuran dehydrogenase subunit A
K00201  formylmethanofuran dehydrogenase subunit B
K00202  formylmethanofuran dehydrogenase subunit C
K00203  formylmethanofuran dehydrogenase subunit D
K11261  formylmethanofuran dehydrogenase subunit E
KLL: BJF97_31235
CAMA: F384_27340
CIR: C2U53_01745
SOF: NCTC11214_05193(dmsA_7)
MCA: MCA2319 MCA2857 MCA2859 MCA2860
METU: GNH96_03545 GNH96_03550 GNH96_03560 GNH96_11470
MMT: Metme_0667 Metme_0669 Metme_0670
MDN: JT25_013490 JT25_013500 JT25_013505
MDH: AYM39_03055 AYM39_03085 AYM39_03090
MKO: MKLM6_0652 MKLM6_0658 MKLM6_0659
BXE: Bxe_B2461(fhcB) Bxe_B2462(fhcA) Bxe_B2464(fhcC)
RGE: RGE_40380(fhcB) RGE_40400(fhcA) RGE_40420(fhcC)
MEP: MPQ_1569(fwdB) MPQ_1570(fwdA) MPQ_1572(fwdC)
AZA: AZKH_p0239(fhcC) AZKH_p0241(fhcA) AZKH_p0242(fhcB)
SDL: Sdel_0813
GBM: Gbem_1223
GEM: GM21_3052
PCA: Pcar_0156
DEU: DBW_2934
DVL: Dvul_2793
DVM: DvMF_1613
DMA: DMR_08200(fmdE) DMR_21490(fwdE)
DOL: Dole_0190
MEA: Mex_1p1755(fhcC) Mex_1p1757(fhcA) Mex_1p1758(fhcB)
MDI: METDI2507(fhcC) METDI2509(fhcA) METDI2510(fhcB)
HMC: HYPMC_1886(fhcC) HYPMC_1888(fhcA) HYPMC_1889
PLEO: OHA_1_00508(fhcC) OHA_1_00510(fhcA) OHA_1_00511(fhcB)
HDI: HDIA_2303(fhcC) HDIA_2305(fhcA)
CBO: CBO1674
CBA: CLB_1687
CBH: CLC_1695
CBY: CLM_1911
CBL: CLK_1133
CBB: CLD_2887
CBI: CLJ_B1863
CACE: CACET_c07900(fwdE)
AMT: Amet_1509
SWO: Swol_1664
SLP: Slip_0379
DAE: Dtox_1669
PTH: PTH_1484
DAU: Daud_1104
SGY: Sgly_3097
HMO: HM1_1872
SAY: TPY_3706(fmdE) TPY_3733(fmdE)
TTE: TTE1865
CHY: CHY_2194
MTA: Moth_1467
ADG: Adeg_1196
TPZ: Tph_c01530 Tph_c22380(ftsZ2)
CSC: Csac_0177
CBAC: JI75_04760
CYB: CYB_0846
LET: O77CONTIG1_00376(gltS_1)
DET: DET1173
RCA: Rcas_2175
CAU: Caur_0027
CAG: Cagg_3664
DRA: DR_A0267
DFC: DFI_12385
RBA: RB9834(fwdA) RB9836(fwdC)
PIR: VN12_00235(fhcA) VN12_04740(fhcC)
RUL: UC8_09140(fhcA) UC8_09160(fhcC) UC8_25590
PEH: Spb1_21210(fhcC) Spb1_25380(fhcA) Spb1_30750
PLS: VT03_03470(fhcA) VT03_09455(fhcB) VT03_21690(fhcC)
PLH: VT85_05440 VT85_05445(fhcA) VT85_05460(fhcC)
GES: VT84_05715 VT84_21855(fhcC) VT84_26835(fhcA)
PBOR: BSF38_00164(fhcC) BSF38_00167(fhcA) BSF38_00168(fhcB)
AGV: OJF2_59240(fhcB) OJF2_59250(fhcA) OJF2_59270(fhcC)
ACA: ACP_1857
SUS: Acid_6374
TLI: Tlie_0301
CTE: CT1717
IAL: IALB_2829(fmdE) IALB_2832(fmdE)
TTK: TST_1595(fmdE)
DTU: Dtur_0248
CTHI: THC_1152
MMP: MMP0070 MMP0200(fmdE) MMP0508(fmdE) MMP0509(fmdA) MMP0510(fmdC) MMP0511(fmdB) MMP0512(fmdB) MMP0965 MMP1247(fwdD) MMP1248(fwdA) MMP1249(fwdC) MMP1691(fwdB)
MST: Msp_0242(fwdD) Msp_0243(fwdB) Msp_0244(fwdA) Msp_0245(fwdC)
MRU: mru_0254(fwdE) mru_0342(fwdD) mru_0343(fwdB) mru_0344(fwdA) mru_0345(fwdC)
MEB: Abm4_0140(fwdD) Abm4_0141(fwdB) Abm4_0142(fwdA) Abm4_0143(fwdC) Abm4_0145(fwdE)
MMIL: sm9_2172(fwdC) sm9_2173(fwdA) sm9_2174(fwdB) sm9_2175(fwdD) sm9_2185(fwdE)
MFC: BRM9_0176(fwdD) BRM9_0177(fwdB) BRM9_0178(fwdA) BRM9_0179(fwdC) BRM9_0202(fwdE1) BRM9_0205(fwdE2) BRM9_0573 BRM9_2342(fwdE3) BRM9_2346(fwdE4)
MCUB: MCBB_0128(fwdD) MCBB_0129(fwdA) MCBB_0130(fwdC1) MCBB_0131(fwdB) MCBB_1586 MCBB_2290
MKA: MK0259(fwdB_1) MK1526(fwdD) MK1527(fwdB_2) MK1529(fwdA) MK1530(fwdC)
TAC: Ta1109
TVO: TVG0674383(TVG0674383)
CDIV: CPM_1801
PFU: PF0913
PFI: PFC_03785
PHO: PH1238(PH1238)
PAB: PAB0675
PYN: PNA2_1681
PYS: Py04_0831
TON: TON_0257
TSI: TSIB_1861
THE: GQS_08100
THM: CL1_1242
TLT: OCC_01179
PPAC: PAP_08665
MAC: MA_0304(fmdE) MA_0306(fmdA) MA_0307(fmdC) MA_0308(fmdD) MA_0309(fmdB) MA_0381(fwdE) MA_0832(fwdC) MA_0833(fwdA) MA_0834(fwdB) MA_0835(fwuD) MA_1241(fmdB) MA_2878(fwdB) MA_2879(fwdD) MA_4175(fmdA) MA_4176(fmdC) MA_4177(fmdD) MA_4178(fmdB) MA_4602(fwdE)
MBG: BN140_1254(fwdD1) BN140_1255(fwdB1) BN140_1256(fwdA1) BN140_1257(fwdC1) BN140_1525(fwdD3) BN140_1526(fwdB3) BN140_1527(fwdA3) BN140_1528(fwdC3) BN140_1730(fwdD5) BN140_1731(fwdB5) BN140_1732(fwdA5) BN140_1733(fwdC5) BN140_2199(fmdE) BN140_2354 BN140_2508(fwdE)
MPD: MCP_1081 MCP_1571(fwdC-1) MCP_1572(fwdA-1) MCP_1573(fwdB-1) MCP_1574(fwdD-1) MCP_2763(fwdC-2) MCP_2764(fwdA-2) MCP_2765(fwdB-2) MCP_2766(fwdD-2)
MEZ: Mtc_0156(fwdE-1) Mtc_0160(fmdE) Mtc_0163(fmdB) Mtc_0164(fmdD) Mtc_1680(fwdE-2) Mtc_1818(fwdE-3) Mtc_2468(fwdC) Mtc_2469(fwdA) Mtc_2470(fwdB) Mtc_2471(fwdD)
RCI: RCIX1003 RCIX1392(fwdE) RCIX1639(fmdE) RCIX1641(fmdB) RCIX1642(fmdD) RCIX598(fwdD-1) RCIX599(fwdB-1) RCIX600(fwdA-1) RCIX601(fwdC-1) RRC260(fwdD-2) RRC261(fwdB-2) RRC262(fwdA-2) RRC263(fwdC-2)
HALA: Hrd1104_05250(tsaA)
HARC: HARCEL1_00445(tsaA)
DKA: DKAM_1436
SIH: SiH_0907
PIS: Pisl_0219
TPE: Tpen_1423
NDV: NDEV_0843(fmdE)
BARC: AOA65_2055(fwdC) AOA65_2056 AOA65_2057(fdhA) AOA65_2058(fmdC)
 » show all
1  [PMID:2125267]
Karrasch M, Borner G, Enssle M, Thauer RK.
The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor.
Eur J Biochem 194:367-72 (1990)
2  [PMID:8161283]
Bertram PA, Schmitz RA, Linder D, Thauer RK
Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme  of formylmethanofuran dehydrogenase.
Arch Microbiol 161:220-8 (1994)
3  [PMID:8125106]
Bertram PA, Karrasch M, Schmitz RA, Bocher R, Albracht SP, Thauer RK
Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins.
Eur J Biochem 220:477-84 (1994)
4  [PMID:9342247]
Vorholt JA, Thauer RK
The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea.
Eur J Biochem 248:919-24 (1997)
5  [PMID:11929975]
Meuer J, Kuettner HC, Zhang JK, Hedderich R, Metcalf WW
Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central  role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation.
Proc Natl Acad Sci U S A 99:5632-7 (2002)
6  [PMID:21262829]
Kaster AK, Moll J, Parey K, Thauer RK
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in  hydrogenotrophic methanogenic archaea.
Proc Natl Acad Sci U S A 108:2981-6 (2011)
7  [PMID:27846502]
Wagner T, Ermler U, Shima S
The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters.
Science 354:114-117 (2016)
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 119940-12-4

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