HDRB2_METMP
ID HDRB2_METMP Reviewed; 293 AA.
AC Q6LYD8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=H(2)/formate:CoB-CoM heterodisulfide,ferredoxin reductase subunit B2 {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 B2 {ECO:0000305};
GN Name=hdrB2 {ECO:0000303|PubMed:20534465};
GN OrderedLocusNames=MMP1053 {ECO:0000312|EMBL:CAF30609.1};
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; CAF30609.1; -; Genomic_DNA.
DR RefSeq; WP_011170997.1; NC_005791.1.
DR AlphaFoldDB; Q6LYD8; -.
DR SMR; Q6LYD8; -.
DR STRING; 267377.MMP1053; -.
DR EnsemblBacteria; CAF30609; CAF30609; MMP1053.
DR GeneID; 2761166; -.
DR KEGG; mmp:MMP1053; -.
DR PATRIC; fig|267377.15.peg.1086; -.
DR eggNOG; arCOG00338; Archaea.
DR HOGENOM; CLU_052147_1_0_2; -.
DR OMA; PGCVAQG; -.
DR OrthoDB; 73750at2157; -.
DR BioCyc; MMAR267377:MMP_RS05445-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..293
FT /note="H(2)/formate:CoB-CoM heterodisulfide,ferredoxin
FT reductase subunit B2"
FT /id="PRO_0000443937"
SQ SEQUENCE 293 AA; 32026 MW; EE8526BB154A955B CRC64;
MKYAFFLGCI MPNRYAGVES ATRTVMEKLG VELVDMPGAS CCPAPGVFGS FDQKTWLTLA
ARNLVIAEEM GTDIVTVCNG CYGSLYEAAH MLHENKEALA MVNEQLKEIG KEYKGTVHVR
HFAELIYKEI GVDKIRENVV KPLAVNIGVH YGCHFLKPTA AKGLGNAEHP TMLDELVEAT
GAKSVDYKDK MMCCGAGGGV RAKELDLALS MTQEKIENML AVGADATVNV CPFCQLQFDR
GQVEIKEKLG NEYNFPVVHL SQLLGLAMGM DPKEVALDVN FISPEPLLQK LGY
