KEGG   ENZYME: 1.8.98.5Help
Entry
EC 1.8.98.5                 Enzyme                                 

Name
H2:CoB-CoM heterodisulfide,ferredoxin reductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With other, known, physiological acceptors
BRITE hierarchy
Sysname
CoB,CoM,ferredoxin:H2 oxidoreductase
Reaction(IUBMB)
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB [RN:R11943]
Reaction(KEGG)
Substrate
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
CoB [CPD:C04628];
CoM [CPD:C03576];
H+ [CPD:C00080]
Product
H2 [CPD:C00282];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
CoM-S-S-CoB [CPD:C04832]
Comment
This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its delta subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
History
EC 1.8.98.5 created 2017
Pathway
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K03388  heterodisulfide reductase subunit A2
K03389  heterodisulfide reductase subunit B2
K03390  heterodisulfide reductase subunit C2
K14126  F420-non-reducing hydrogenase large subunit
K14127  F420-non-reducing hydrogenase iron-sulfur subunit
K14128  F420-non-reducing hydrogenase small subunit
Genes
TIG: THII_2280
TVI: Thivi_3111
TMB: Thimo_0247 Thimo_0248 Thimo_0253
TSY: THSYN_16425
HHC: M911_11215 M911_11220 M911_11230 M911_11235 M911_11240
EBS: ECTOBSL9_0282 ECTOBSL9_0283 ECTOBSL9_0285 ECTOBSL9_0286 ECTOBSL9_0287
TGR: Tgr7_2211 Tgr7_2212 Tgr7_2214 Tgr7_2215 Tgr7_2216
TKM: TK90_0632 TK90_0633 TK90_0634 TK90_0636 TK90_0637
TNI: TVNIR_3244(hdrB_[H]) TVNIR_3245(hdlC_[H]) TVNIR_3247(hdrA_[H]) TVNIR_3248(hdlB_[H]) TVNIR_3249
TVR: TVD_10625 TVD_10630 TVD_10640 TVD_10645 TVD_10650
SLIM: SCL_2520
TBN: TBH_C2777
ENM: EBS_2145(hdrB)
CBX: Cenrod_2144(mvhG) Cenrod_2145(mvhA) Cenrod_2147(hdrA) Cenrod_2148(mvhD)
SHD: SUTH_02769(hdrB)
TBD: Tbd_1645
SDR: SCD_n01881(hdrB)
GSU: GSU0090(hdrA) GSU0091(hdrB) GSU0092(hdrC) GSU2418(mvhS) GSU2419(mvhL)
GSK: KN400_0065(hdrA) KN400_0066(hdrB) KN400_0067(hdrC) KN400_2366(mvhS) KN400_2367(mvhL)
GME: Gmet_2084(bamE) Gmet_3319(mvhS) Gmet_3320(mvhL) Gmet_3424(hdrC) Gmet_3425(hdrB) Gmet_3426(hdrA)
GBM: Gbem_0030(hdrA) Gbem_0031(hdrB) Gbem_0032(hdrC) Gbem_1447(bamE) Gbem_3884(mvhL) Gbem_3885(mvhS)
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_11730(mvhG) HRM2_11740(mvhA) HRM2_11850(hdrA2) HRM2_22720(hdrL2) HRM2_22750(hdrA4) HRM2_22760(hdrD2) HRM2_22770(hdrD2')
DTO: TOL2_C02630 TOL2_C03750(bamE1) TOL2_C08890 TOL2_C11590(hdlA2) TOL2_C11600(mvhD2) TOL2_C11630(hdlA3?) TOL2_C11640(mvhD3) TOL2_C17880(mvhD4) TOL2_C17900(hdlA5) TOL2_C17910(hdlC) TOL2_C17920(hdlB) TOL2_C24180(hdlA6) TOL2_C25730(hdlA7) TOL2_C28760(hdlA8) TOL2_C28830(hdlA9) TOL2_C41400(bamE2) TOL2_C43540(bamE3)
SAT: SYN_00626
ATX: GCD22_01577(hdrB1) GCD22_02661(hdrB1) GCD22_03145(hdrB) GCD22_03146(hdlC) GCD22_03148(hdrA) GCD22_03149(hdrB1) GCD22_03150 GCD22_03192(hdrB1) GCD22_03279(hdrA)
PTH: PTH_1410(HdrA) PTH_1412(HdrB) PTH_1413(GlpC)
STED: SPTER_13740 SPTER_13750(sdhE_1) SPTER_13760(mnmC)
DEV: DhcVS_552(vhuG) DhcVS_553(vhuA)
DMC: btf_574(vhcG) btf_575(vhcA)
DMD: dcmb_620(vhcG) dcmb_621(vhcA)
DMG: GY50_0540(mvhG) GY50_0541(mvhA)
DFO: Dform_00920(hdrA) Dform_00937(mvhA|vhcA) Dform_00938(mvhG|vhcG) 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)
CTHI: THC_1756
MMP: MMP0821(vhcD) MMP0822(vhcG) MMP0823(vhcA) MMP0825(hdrA) MMP1053(hdrB2) MMP1054(hdrC2) MMP1154(hdrC1) MMP1155(hdrB1) MMP1694(vhuA) MMP1695(vhuG) MMP1696(vhuD) MMP1697(hdrA)
MWO: MWSIV6_0409(hdrC) MWSIV6_0410(hdrB) MWSIV6_1526(mvhA) MWSIV6_1527(mvhG) MWSIV6_1528(mvhD) MWSIV6_1530(vhcD) MWSIV6_1762(hdrA)
MST: Msp_0314(mvhD1) Msp_0315(mvhG) Msp_0316(mvhA) Msp_0638(mvhD2) Msp_1013(hdrB1) Msp_1014(hdrC1) Msp_1476(hdrA1)
MRU: mru_0117(hdrA) mru_0816(hdrC) mru_0817(hdrB1) mru_1906(mvhA) mru_1907(mvhG) mru_1908(mvhD1) mru_2076(mvhD2)
MEB: Abm4_0853(mvhD2) Abm4_1308(hdrB2) Abm4_1309(hdrC2) Abm4_1510(mvhA) Abm4_1511(mvhG) Abm4_1512(mvhD) Abm4_1691(hdrA2)
MMIL: sm9_1348(flpD) sm9_1716(hdrB3) sm9_1717(hdrC2) sm9_2011(mvhA) sm9_2012(mvhG) sm9_2013(mvhD) sm9_2251(hdrA2)
MFC: BRM9_0490(hdrB1) BRM9_0491(hdrC1) BRM9_0562(mvhG1) BRM9_0563(mvhA1) BRM9_0913(mvhA2) BRM9_0914(mvhG2) BRM9_0915(mvhD) BRM9_2298(hdrA2)
MCUB: MCBB_1489(hdrB3) MCBB_1490(hdrC3) MCBB_1579(vhuG) MCBB_1580(vhcA) MCBB_1966(mvhA) MCBB_1967(mvhG) MCBB_1968(mvhD) MCBB_2030(vhcD) MCBB_2243(hdrA3)
MKA: MK0178 MK0179 MK0249(hdrA_1) MK0265(hdrA_2) MK0266 MK0267 MK0268(flpD_1) MK0572(hdrB) MK0573(hdrC) MK0627(flpD_2)
MEAR: Mpt1_c02960(hdrC1) Mpt1_c02970(hdrB1) Mpt1_c08830(hdrB2) Mpt1_c08840(hdrC2) Mpt1_c10550(mvhA) Mpt1_c10560(mvhG) Mpt1_c10570(vhcD) Mpt1_c10580(hdrA)
MAC: MA_2868(hdrA) MA_4236(hdrC) MA_4237(hdrB)
MBU: Mbur_0552(hdrA) Mbur_1516(hdrC) Mbur_1517(hdrB)
MCJ: MCON_3279(hdrA) MCON_3282(hdrC) MCON_3283(hdrB)
MBG: BN140_0752(hdrA1) BN140_1726(hdrC) BN140_1727(hdrB) BN140_1728(hdrA3) BN140_1834(mvhG) BN140_1835(mvhA)
MEMA: MMAB1_0971(hdrA) MMAB1_2221(hdrC) MMAB1_2222(hdrB) MMAB1_2223(hdrA) MMAB1_2367(vhcG) MMAB1_2368(vhcA)
MPD: MCP_1576(hdrA-1) MCP_1577(hdrB-1) MCP_1578(hdrC-1) MCP_2492(mvhA-1) MCP_2493(mvhG-1) MCP_2767(mvhD-2) MCP_2768(hdrA-2) MCP_2769(hdrB-3) MCP_2770(hdrC-3) MCP_2773(mvhG-2) MCP_2774(mvhA-2)
MEZ: Mtc_0109(mvhA-1) Mtc_0111(mvhG-1) Mtc_2472(mvhD-2) Mtc_2473(hdrA-2) Mtc_2474(hdrB-2) Mtc_2475(hdrC-2) Mtc_2478(mvhG-2) Mtc_2479(mvhA-2)
RCI: RCIX473(mvhA-1) RCIX474(mvhG-1) RCIX590(mvhA-2) RCIX591(mvhG-2) RCIX594(hdrC-2) RCIX595(hdrB-2) RCIX596(hdrA-2) RCIX597(mvhD-1) RRC256(hdrC-3) RRC257(hdrB-3) RRC258(hdrA-3)
HDF: AArcSl_1855(hdrA)
SSO: SSO1127(hdrC-1) SSO1129(hdrB-1) SSO1131(hdrA) SSO1134(hdrC-2) SSO1135(hdrB-2)
BARC: AOA65_0030(hdrC_1) AOA65_1112(hdrA_1) AOA65_1400(hdrC_2) AOA65_1401(hdrB_2) AOA65_1402(hdrA_3) AOA65_1715(mvhD_1) AOA65_1718(mvhD_2) AOA65_1719(hdlA_2) AOA65_1722 AOA65_1723 AOA65_1885(mvhA) AOA65_1886(mvhG) 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_1505(mvhA_2) AOA66_1506(mvhG) 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:2654933]
  Authors
Reeve JN, Beckler GS, Cram DS, Hamilton PT, Brown JW, Krzycki JA, Kolodziej AF, Alex L, Orme-Johnson WH, Walsh CT
  Title
A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain delta H  encodes a polyferredoxin.
  Journal
Proc Natl Acad Sci U S A 86:3031-5 (1989)
DOI:10.1073/pnas.86.9.3031
  Sequence
Reference
2  [PMID:7925445]
  Authors
Hedderich R, Koch J, Linder D, Thauer RK
  Title
The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains  sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases.
  Journal
Eur J Biochem 225:253-61 (1994)
DOI:10.1111/j.1432-1033.1994.00253.x
  Sequence
Reference
3  [PMID:8119281]
  Authors
Setzke E, Hedderich R, Heiden S, Thauer RK
  Title
H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties.
  Journal
Eur J Biochem 220:139-48 (1994)
DOI:10.1111/j.1432-1033.1994.tb18608.x
Reference
4  [PMID:12856108]
  Authors
Stojanowic A, Mander GJ, Duin EC, Hedderich R
  Title
Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis.
  Journal
Arch Microbiol 180:194-203 (2003)
DOI:10.1007/s00203-003-0577-9
  Sequence
Reference
5  [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
6  [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: 1.8.98.5
IUBMB Enzyme Nomenclature: 1.8.98.5
ExPASy - ENZYME nomenclature database: 1.8.98.5
BRENDA, the Enzyme Database: 1.8.98.5

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