KEGG   ENZYME: 1.2.7.12
Entry
EC 1.2.7.12                 Enzyme                                 

Name
formylmethanofuran dehydrogenase;
formylmethanofuran:acceptor oxidoreductase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With an iron-sulfur protein as acceptor
Sysname
formylmethanofuran:ferredoxin oxidoreductase
Reaction(IUBMB)
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ [RN:R11743]
Reaction(KEGG)
R11743 > R03015;
(other) R08060
Substrate
formylmethanofuran [CPD:C01001];
H2O [CPD:C00001];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139]
Product
CO2 [CPD:C00011];
methanofuran [CPD:C00862];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080]
Comment
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.
History
EC 1.2.7.12 created 1992 as EC 1.2.99.5, transferred 2017 to EC 1.2.7.12
Pathway
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
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
Genes
MCA: MCA2319 MCA2857 MCA2859 MCA2860
METU: GNH96_03545 GNH96_03550 GNH96_03560
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
METL: U737_16710 U737_20580 U737_20585 U737_20595
MPAD: KEF85_01260 KEF85_01270 KEF85_01275
MAH: MEALZ_0829 MEALZ_1262 MEALZ_1263(fhcA) MEALZ_1270
MBUR: EQU24_08915 EQU24_08920 EQU24_08950 EQU24_16910
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
GEO: Geob_2236
PPD: Ppro_2088
DVU: DVU_0175
DVL: Dvul_2793
DVM: DvMF_1613
DMA: DMR_08200(fmdE) DMR_21490(fwdE)
DSF: UWK_02749
DOL: Dole_0190
DML: Dmul_03690(fwdE)
DTO: TOL2_C00550(fwdE) TOL2_C05380(fwdE2)
DLI: dnl_54910
SFU: Sfum_0032
DBR: Deba_3073
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) HDIA_2306(fhcB)
CBO: CBO1674
CBA: CLB_1687
CBH: CLC_1695
CBY: CLM_1911
CBL: CLK_1133
CBB: CLD_2887
CBI: CLJ_B1863
CSQ: CSCA_3565
CACE: CACET_c07900(fwdE)
AMT: Amet_1509
SLP: Slip_0379
DSY: DSY0393
DHD: Dhaf_0346
DAE: Dtox_1669
PTH: PTH_1484
DAU: Daud_1104
SGY: Sgly_3097
HMO: HM1_1872
ELM: ELI_4462
CTHM: CFE_1849
TTE: TTE1865
CHY: CHY_2194
MTA: Moth_1467
ADG: Adeg_1196
TPZ: Tph_c22380(ftsZ2)
CSC: Csac_0177
CBAC: JI75_04760
DET: DET1173
RBA: RB9834(fwdA) RB9836(fwdC)
PIR: VN12_00235(fhcA) VN12_04740(fhcC)
RUL: UC8_09140(fhcA) UC8_09160(fhcC) UC8_25590
ROL: CA51_00140(fhcB) CA51_11980(fhcC) CA51_11990(fhcA)
AHEL: Q31a_04490(fhcA) Q31a_04510(fhcC)
AAGG: ETAA8_14440(fhcB) ETAA8_26970(fhcA) ETAA8_52830(fhcC)
BVO: Pan97_04780(fhcC) Pan97_05410(fhcB) Pan97_18580(fhcA)
AMUC: Pan181_05550(fhcC) Pan181_07630(fhcA) Pan181_07660(fhcB)
PND: Pla175_02540(fhcC) Pla175_10860(fhcA) Pla175_10990(fhcB)
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)
GPN: Pan110_20010(fhcC) Pan110_26670(fhcB) Pan110_37150(fhcA)
MRI: Mal4_07870 Mal4_34120(fhcC) Mal4_34320(fhcA) Mal4_35820(fdhF_2) Mal4_58140(nasA)
PLON: Pla110_09560(fdhF_1) Pla110_21890(fhcA) Pla110_31350(fhcC)
GES: VT84_05715 VT84_21855(fhcC) VT84_26835(fhcA)
ULI: ETAA1_19200(fhcC_1) ETAA1_28600(fhcA_1) ETAA1_48420 ETAA1_48450(fhcA_2) ETAA1_48460(fhcC_2) ETAA1_48640(fhcB)
PBOR: BSF38_00164(fhcC) BSF38_00167(fhcA) BSF38_00168(fhcB)
AGV: OJF2_59240(fhcB) OJF2_59250(fhcA) OJF2_59270(fhcC)
TLI: Tlie_0301
DTU: Dtur_0248
MMP: MMP0200(fmdE) MMP0508(fmdE) MMP0509(fmdA) MMP0510(fmdC) MMP0511(fmdB) MMP0512(fmdB) MMP0965 MMP1247(fwdD) MMP1248(fwdA) MMP1249(fwdC) MMP1691(fwdB)
METE: tca_00881 tca_00882(fhcC_1) tca_00883(fdhF_1) tca_01298 tca_01505 tca_01506(fhcA) tca_01507(fhcC_2) tca_01508(fdhF_3)
MST: Msp_0242(fwdD) Msp_0243(fwdB) Msp_0244(fwdA) Msp_0245(fwdC)
MRU: 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)
MMIL: sm9_2172(fwdC) sm9_2173(fwdA) sm9_2174(fwdB) sm9_2175(fwdD)
METH: MBMB1_0112 MBMB1_0113(fwdB) MBMB1_0114(fwdA) MBMB1_0115(fwdC) MBMB1_0134 MBMB1_1993(fwdE-3) MBMB1_1997(fwdE-4)
MFC: BRM9_0176(fwdD) BRM9_0177(fwdB) BRM9_0178(fwdA) BRM9_0179(fwdC) BRM9_0202(fwdE1) BRM9_2342(fwdE3) BRM9_2346(fwdE4)
MCUB: MCBB_0128(fwdD) MCBB_0129(fwdA) MCBB_0130(fwdC1) MCBB_0131(fwdB) MCBB_2290
MKA: MK0259(fwdB_1) MK1526(fwdD) MK1527(fwdB_2) MK1529(fwdA) MK1530(fwdC)
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)
MCJ: MCON_0238(fmdB) MCON_0239(fmdD) MCON_0240(fmdC) MCON_0241(fmdA) MCON_1733(fwdB) MCON_1734(fwdD) MCON_2129 MCON_2898(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)
BARC: AOA65_2055(fwdC) AOA65_2056 AOA65_2057(fdhA) AOA65_2058(fmdC)
 » show all
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 194:367-72 (1990)
DOI:10.1111/j.1432-1033.1990.tb15627.x
Reference
2  [PMID:8161283]
  Authors
Bertram PA, Schmitz RA, Linder D, Thauer RK
  Title
Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme  of formylmethanofuran dehydrogenase.
  Journal
Arch Microbiol 161:220-8 (1994)
DOI:10.1007/bf00248696
Reference
3  [PMID:8125106]
  Authors
Bertram PA, Karrasch M, Schmitz RA, Bocher R, Albracht SP, Thauer RK
  Title
Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins.
  Journal
Eur J Biochem 220:477-84 (1994)
DOI:10.1111/j.1432-1033.1994.tb18646.x
Reference
4  [PMID:9342247]
  Authors
Vorholt JA, Thauer RK
  Title
The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea.
  Journal
Eur J Biochem 248:919-24 (1997)
DOI:10.1111/j.1432-1033.1997.00919.x
Reference
5  [PMID:11929975]
  Authors
Meuer J, Kuettner HC, Zhang JK, Hedderich R, Metcalf WW
  Title
Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central  role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation.
  Journal
Proc Natl Acad Sci U S A 99:5632-7 (2002)
DOI:10.1073/pnas.072615499
Reference
6  [PMID:21262829]
  Authors
Kaster AK, Moll J, Parey K, Thauer RK
  Title
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in  hydrogenotrophic methanogenic archaea.
  Journal
Proc Natl Acad Sci U S A 108:2981-6 (2011)
DOI:10.1073/pnas.1016761108
Reference
7  [PMID:27846502]
  Authors
Wagner T, Ermler U, Shima S
  Title
The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters.
  Journal
Science 354:114-117 (2016)
DOI:10.1126/science.aaf9284
Other DBs
ExplorEnz - The Enzyme Database: 1.2.7.12
IUBMB Enzyme Nomenclature: 1.2.7.12
ExPASy - ENZYME nomenclature database: 1.2.7.12
BRENDA, the Enzyme Database: 1.2.7.12
CAS: 119940-12-4
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