KEGG   ENZYME: 1.8.98.6Help
Entry
EC 1.8.98.6                 Enzyme                                 

Name
formate:CoB-CoM heterodisulfide,ferredoxin reductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With other, known, physiological acceptors
BRITE hierarchy
Sysname
coenzyme B,coenzyme M,ferredoxin:formate oxidoreductase
Reaction(IUBMB)
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB [RN:R11944]
Reaction(KEGG)
Substrate
CO2 [CPD:C00011];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
CoB [CPD:C04628];
CoM [CPD:C03576];
H+ [CPD:C00080]
Product
formate [CPD:C00058];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
CoM-S-S-CoB [CPD:C04832]
Comment
The enzyme is found in formate-oxidizing CO2-reducing methanogenic archaea such as Methanococcus maripaludis. It consists of a cytoplasmic complex of HdrABC reductase and formate dehydrogenase. Electron pairs donated by formate dehydrogenase are transferred to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
History
EC 1.8.98.6 created 2017
Pathway
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K00125  formate dehydrogenase (coenzyme F420) beta subunit
K03388  heterodisulfide reductase subunit A2
K03389  heterodisulfide reductase subunit B2
K03390  heterodisulfide reductase subunit C2
K14127  F420-non-reducing hydrogenase iron-sulfur subunit
K22516  formate dehydrogenase (coenzyme F420) alpha subunit
Genes
VNA: PN96_21155
VEJ: VEJY3_20411
PGB: H744_1c0419
PSH: Psest_3905
PSTU: UIB01_19765
PBM: CL52_01700
PCH: EY04_14750
PSED: DM292_16890
GNI: GNIT_2862
TIG: THII_2280
TNI: TVNIR_3244(hdrB_[H]) TVNIR_3245(hdlC_[H]) TVNIR_3247(hdrA_[H]) TVNIR_3248(hdlB_[H]) TVNIR_3249
SLIM: SCL_2520
TBN: TBH_C2777
ENM: EBS_2145(hdrB)
CBX: Cenrod_2147(hdrA) Cenrod_2148(mvhD)
SHD: SUTH_02769(hdrB)
TBD: Tbd_1645
SDR: SCD_n01881(hdrB)
CGRA: CGRAC_1361(fdhH)
CPIN: CPIN18020_0262(fdhH)
GSU: GSU0090(hdrA) GSU0091(hdrB) GSU0092(hdrC)
GSK: KN400_0065(hdrA) KN400_0066(hdrB) KN400_0067(hdrC)
GME: Gmet_2084(bamE) Gmet_3424(hdrC) Gmet_3425(hdrB) Gmet_3426(hdrA)
GBM: Gbem_0030(hdrA) Gbem_0031(hdrB) Gbem_0032(hdrC) Gbem_1447(bamE)
GEO: Geob_0215(bamE-1) Geob_0231(bamE-2) Geob_3723(hdrA) Geob_3724(hdrB) Geob_3725(hdrC)
DVU: DVU2402(hdrA) DVU2403(hdrB) DVU2404(hdrC)
DMA: DMR_01900(hdrC) DMR_01910(hdrB) DMR_01920(hdrA) DMR_22120
DGG: DGI_1048(hdrC) DGI_1049(hdrB) DGI_1050(hdrA)
DTR: RSDT_0565(hdrC) RSDT_0566(hdrB) RSDT_0567(hdrA)
DPI: BN4_10653 BN4_11858(hdrC) BN4_11859(hdrB) BN4_11860(hdrA)
PPRF: DPRO_3258
DML: Dmul_02770(hdrA1) Dmul_24500(bamE) Dmul_28860(hdrA2) Dmul_28870(hdrB) Dmul_28880(hdrC)
DAT: HRM2_11710(hdrA1) HRM2_11720(mvhD2) HRM2_11850(hdrA2) HRM2_22720(hdrL2) HRM2_22740(fdhB6) HRM2_22750(hdrA4) HRM2_22760(hdrD2) HRM2_22770(hdrD2')
ADE: Adeh_4164
SAT: SYN_00626
PTH: PTH_1410(HdrA) PTH_1412(HdrB) PTH_1413(GlpC)
DFO: Dform_00920(hdrA) Dform_00940(mvhD|vhcD) Dform_00941(hdrA) Dform_00942(hdrB) Dform_00943(hdrC)
CTE: CT1245 CT1246(hdrA-2)
AAE: aq_391 aq_395(hdrA) aq_398(hdrC) aq_400(hdrB)
HTH: HTH_1878(hdrB1) HTH_1879(hdrC1) HTH_1881(hdrA) HTH_1882(hdrB2) HTH_1883(hdrC2)
MMP: MMP0138(fdhA) MMP0139(fdhB) MMP0821(vhcD) MMP0825(hdrA) MMP1053(hdrB2) MMP1054(hdrC2) MMP1154(hdrC1) MMP1155(hdrB1) MMP1297(fdhB) MMP1298(fdhA) MMP1696(vhuD) MMP1697(hdrA)
MST: Msp_0314(mvhD1) Msp_0638(mvhD2) Msp_0639(fdhB) Msp_0640(fdhA) Msp_1013(hdrB1) Msp_1014(hdrC1) Msp_1476(hdrA1)
MRU: mru_0117(hdrA) mru_0333(fdhA1) mru_0334(fdhB1) mru_0816(hdrC) mru_0817(hdrB1) mru_1908(mvhD1) mru_2074(fdhA2) mru_2075(fdhB2) mru_2076(mvhD2)
MEB: Abm4_0131(fdhA) Abm4_0132(fdhB) Abm4_0853(mvhD2) Abm4_0854(fdhB2) Abm4_0855(fdhA2) Abm4_1308(hdrB2) Abm4_1309(hdrC2) Abm4_1512(mvhD) Abm4_1691(hdrA2)
MMIL: sm9_1348(flpD) sm9_1349(flpB) sm9_1350(flpA) sm9_1716(hdrB3) sm9_1717(hdrC2) sm9_2013(mvhD) sm9_2182(fdhB) sm9_2183(fdhA) sm9_2251(hdrA2)
METH: MBMB1_0103(fdhB) MBMB1_0104(fdhA) MBMB1_1274(hdrB) MBMB1_1275 MBMB1_1663(mvhD) MBMB1_1958(hdrA)
MFC: BRM9_0167(fdhB) BRM9_0168(fdhA) BRM9_0490(hdrB1) BRM9_0491(hdrC1) BRM9_0915(mvhD) BRM9_2298(hdrA2)
MCUB: MCBB_1489(hdrB3) MCBB_1490(hdrC3) MCBB_1968(mvhD) MCBB_2028(fdhA) MCBB_2029(fdhB1) MCBB_2030(vhcD) MCBB_2031(fdhB3) MCBB_2243(hdrA3)
MKA: MK0249(hdrA_1) MK0265(hdrA_2) MK0268(flpD_1) MK0321 MK0322 MK0572(hdrB) MK0573(hdrC) MK0627(flpD_2)
TAC: Ta0045
TVO: TVG0003442(TVG0003442)
MEAR: Mpt1_c02960(hdrC1) Mpt1_c02970(hdrB1) Mpt1_c08830(hdrB2) Mpt1_c08840(hdrC2) Mpt1_c10570(vhcD) Mpt1_c10580(hdrA)
TKO: TK2076
TON: TON_0539
TGA: TGAM_0065(mhy2A)
THE: GQS_02455
THM: CL1_1148
TLT: OCC_12236
THS: TES1_1496
TNU: BD01_1899
PPAC: PAP_03230
MAC: MA_2868(hdrA) MA_4236(hdrC) MA_4237(hdrB)
MBU: Mbur_0552(hdrA) Mbur_1516(hdrC) Mbur_1517(hdrB)
MCJ: MCON_2237(fdhA) MCON_3279(hdrA) MCON_3282(hdrC) MCON_3283(hdrB)
MBG: BN140_0752(hdrA1) BN140_0841(fdhB) BN140_0842(fdhA) BN140_1327(fdhA1) BN140_1328(fdhB1) BN140_1329(fdhA2) BN140_1330(fdhB2) BN140_1726(hdrC) BN140_1727(hdrB) BN140_1728(hdrA3) BN140_2197(fdhB3) BN140_2198(fdhA3)
MEMA: MMAB1_0971(hdrA) MMAB1_1105(fdhB) MMAB1_1106(fdhA) MMAB1_1689(fdhA) MMAB1_1690(fdhB) MMAB1_2221(hdrC) MMAB1_2222(hdrB) MMAB1_2223(hdrA) MMAB1_2913(fdhB) MMAB1_2914(fdhA)
MPD: MCP_1569(fdhB-1) MCP_1570(fdhA-1) MCP_1576(hdrA-1) MCP_1577(hdrB-1) MCP_1578(hdrC-1) MCP_2406(fdhB-2) MCP_2407(fdhA-2) MCP_2767(mvhD-2) MCP_2768(hdrA-2) MCP_2769(hdrB-3) MCP_2770(hdrC-3)
MEZ: Mtc_2124(fdhB) Mtc_2125(fdhA) Mtc_2472(mvhD-2) Mtc_2473(hdrA-2) Mtc_2474(hdrB-2) Mtc_2475(hdrC-2)
RCI: RCIX1628(fdhA-1) RCIX1630(fdhB-1) RCIX2372(fdhB-2) RCIX2373(fdhA-2) RCIX2376(fdhB-3) RCIX2378(fdhA-3) RCIX594(hdrC-2) RCIX595(hdrB-2) RCIX596(hdrA-2) RCIX597(mvhD-1) RRC251(fdhA-4) RRC252(fdhB-4) RRC256(hdrC-3) RRC257(hdrB-3) RRC258(hdrA-3)
SSO: SSO1127(hdrC-1) SSO1129(hdrB-1) SSO1131(hdrA) SSO1134(hdrC-2) SSO1135(hdrB-2)
TPE: Tpen_0190
BARC: AOA65_0029(hdrB_1) AOA65_0030(hdrC_1) AOA65_1112(hdrA_1) AOA65_1193(hdrA_2) AOA65_1400(hdrC_2) AOA65_1401(hdrB_2) AOA65_1402(hdrA_3) AOA65_1718(mvhD_2) AOA65_1719(hdlA_2) AOA65_1887(hdrB_3) AOA65_1888(hdrC_3) AOA65_1889(vhcD) AOA65_1993(hdrB_4) AOA65_1994(hdrC_4) AOA65_1995(hdrA_4)
BARB: AOA66_0155(hdrA_1) AOA66_1507(hdrB_1) AOA66_1508(hdrC_1) AOA66_1509(vhcD) AOA66_1510(hdrA_2) AOA66_1512(hdlA_2) AOA66_1513(hdrA_3) AOA66_1526(hdrA_4) AOA66_1731(hdrB_2) AOA66_1732(hdrC_2)
 » show all
Taxonomy
Reference
1  [PMID:20534465]
  Authors
Costa KC, Wong PM, Wang T, Lie TJ, Dodsworth JA, Swanson I, Burn JA, Hackett M, Leigh JA
  Title
Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase.
  Journal
Proc Natl Acad Sci U S A 107:11050-5 (2010)
DOI:10.1073/pnas.1003653107
Reference
2  [PMID:24039260]
  Authors
Costa KC, Lie TJ, Xia Q, Leigh JA
  Title
VhuD facilitates electron flow from H2 or formate to heterodisulfide reductase in Methanococcus maripaludis.
  Journal
J Bacteriol 195:5160-5 (2013)
DOI:10.1128/JB.00895-13
Other DBs
ExplorEnz - The Enzyme Database: 1.8.98.6
IUBMB Enzyme Nomenclature: 1.8.98.6
ExPASy - ENZYME nomenclature database: 1.8.98.6
BRENDA, the Enzyme Database: 1.8.98.6

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