HDRB1_METMP
ID HDRB1_METMP Reviewed; 301 AA.
AC Q6LY38;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=H(2)/formate:CoB-CoM heterodisulfide,ferredoxin reductase subunit B1 {ECO:0000305};
DE EC=1.8.98.5 {ECO:0000269|PubMed:24039260};
DE EC=1.8.98.6 {ECO:0000269|PubMed:20534465, ECO:0000269|PubMed:24039260};
DE AltName: Full=CoB--CoM heterodisulfide reductase subunit B1 {ECO:0000305};
GN Name=hdrB1 {ECO:0000303|PubMed:20534465};
GN OrderedLocusNames=MMP1155 {ECO:0000312|EMBL:CAF30711.1};
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=S2 / LL;
RX PubMed=20534465; DOI=10.1073/pnas.1003653107;
RA Costa K.C., Wong P.M., Wang T., Lie T.J., Dodsworth J.A., Swanson I.,
RA Burn J.A., Hackett M., Leigh J.A.;
RT "Protein complexing in a methanogen suggests electron bifurcation and
RT electron delivery from formate to heterodisulfide reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11050-11055(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=S2 / LL;
RX PubMed=24039260; DOI=10.1128/jb.00895-13;
RA Costa K.C., Lie T.J., Xia Q., Leigh J.A.;
RT "VhuD facilitates electron flow from H2 or formate to heterodisulfide
RT reductase in Methanococcus maripaludis.";
RL J. Bacteriol. 195:5160-5165(2013).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of
CC CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB
CC (coenzyme B). {ECO:0000269|PubMed:20534465,
CC ECO:0000269|PubMed:24039260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H2 + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55748, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.98.5;
CC Evidence={ECO:0000269|PubMed:24039260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 CO2 + coenzyme B + coenzyme M + 2 reduced [2Fe-2S]-
CC [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 formate + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55752, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.98.6;
CC Evidence={ECO:0000269|PubMed:20534465, ECO:0000269|PubMed:24039260};
CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC heterodisulfide: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: The heterodisulfide reductase is composed of three subunits;
CC HdrA, HdrB and HdrC. B1 and B2 subunits are interchangeable, as are the
CC C1 and C2 subunits. The heterodisulfide reductase forms a supercomplex
CC with formylmethanofuran dehydrogenase (Fwd), F(420)-non-reducing
CC hydrogenase (Vhu) and formate dehydrogenase (Fdh).
CC {ECO:0000269|PubMed:20534465, ECO:0000269|PubMed:24039260}.
CC -!- SIMILARITY: Belongs to the HdrB family. {ECO:0000305}.
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DR EMBL; BX950229; CAF30711.1; -; Genomic_DNA.
DR RefSeq; WP_011171099.1; NC_005791.1.
DR AlphaFoldDB; Q6LY38; -.
DR SMR; Q6LY38; -.
DR STRING; 267377.MMP1155; -.
DR EnsemblBacteria; CAF30711; CAF30711; MMP1155.
DR GeneID; 2761280; -.
DR KEGG; mmp:MMP1155; -.
DR PATRIC; fig|267377.15.peg.1188; -.
DR eggNOG; arCOG00338; Archaea.
DR HOGENOM; CLU_052147_1_0_2; -.
DR OMA; SCCGASH; -.
DR OrthoDB; 73750at2157; -.
DR BioCyc; MetaCyc:MON-20166; -.
DR BioCyc; MMAR267377:MMP_RS05960-MON; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:InterPro.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR017678; CoB/CoM_hetero-S_Rdtase_bsu.
DR InterPro; IPR004017; Cys_rich_dom.
DR Pfam; PF02754; CCG; 2.
DR TIGRFAMs; TIGR03288; CoB_CoM_SS_B; 1.
PE 1: Evidence at protein level;
KW Methanogenesis; Oxidoreductase; Reference proteome.
FT CHAIN 1..301
FT /note="H(2)/formate:CoB-CoM heterodisulfide,ferredoxin
FT reductase subunit B1"
FT /id="PRO_0000443936"
SQ SEQUENCE 301 AA; 33510 MW; E8314823A7BC0235 CRC64;
MSETDFEYMF FLGCIAPNRY PGIESATYKA LDKLGIQLHP FEQASCCPAP GVFGSFDLMT
WLTIAARNIV MAEQADLDIL TICNGCYGSL FEANHILQDN ENARNKVNEV LSKHGLEYTG
KSRVRHLTEV LYFDYGTEKI AERVERPLDI NVAVHYGCHY LKPTDVKHIE SSEVPKSLDG
LVEAIGAKSI YYKDKNMCCG AGGGVRARNP EVALEMAETK VKNIIAAGGD CVTEVCPFCH
LQFDRGQIEM KETFGREYKL PVIHYAQLLG MAMGMTPKEV ALDLHFIPAD PLLEKLGINM
E
