HDRB_METTH
ID HDRB_METTH Reviewed; 302 AA.
AC O27907;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit B {ECO:0000250|UniProtKB:Q50755};
DE EC=1.8.98.5 {ECO:0000250|UniProtKB:Q50755};
DE AltName: Full=CoB--CoM heterodisulfide reductase subunit B {ECO:0000250|UniProtKB:Q50755};
GN Name=hdrB; OrderedLocusNames=MTH_1879;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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:0000250|UniProtKB:Q50755}.
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:0000250|UniProtKB:Q50755};
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:0000250|UniProtKB:Q50755}.
CC -!- SUBUNIT: The heterodisulfide reductase is composed of three subunits;
CC HdrA, HdrB and HdrC. It forms a complex with the F420-non-reducing
CC hydrogenase (Mvh), which provides the reducing equivalents to the
CC heterodisulfide reductase. {ECO:0000250|UniProtKB:Q50755}.
CC -!- SIMILARITY: Belongs to the HdrB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000666; AAB86345.1; -; Genomic_DNA.
DR PIR; D69118; D69118.
DR RefSeq; WP_010877481.1; NC_000916.1.
DR AlphaFoldDB; O27907; -.
DR SMR; O27907; -.
DR IntAct; O27907; 1.
DR STRING; 187420.MTH_1879; -.
DR EnsemblBacteria; AAB86345; AAB86345; MTH_1879.
DR GeneID; 1470964; -.
DR KEGG; mth:MTH_1879; -.
DR PATRIC; fig|187420.15.peg.1834; -.
DR HOGENOM; CLU_052147_1_0_2; -.
DR OMA; PGCVAQG; -.
DR BioCyc; MetaCyc:HDRBMAUTO-MON; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000005223; 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 3: Inferred from homology;
KW Methanogenesis; Oxidoreductase; Reference proteome.
FT CHAIN 1..302
FT /note="H(2):CoB-CoM heterodisulfide,ferredoxin reductase
FT subunit B"
FT /id="PRO_0000150069"
SQ SEQUENCE 302 AA; 33513 MW; 1BE40A77DE7DDFDC CRC64;
MEIAYFLGCI MNNRYPGIEK ATRVLFDKLG IELKDMEGAF CCPAPGVFGS FDKTTWAAIA
ARNITIAEEM GSDVMTECNG CFGSLFEANH LLKEDEEMRA KINEILKEAG REYKGEINVR
HLAEILYNDV GLDKLSEVVE KPLNLNVAVH YGCHFLKPSE EINIDNPERP TILDELVEVT
GAKSVDYKDK MMCCGAGGGV RSRDLDVALD FTMEKLRNMK EAGVDAIVNV CPFCHLQFDV
GQMEIKDKFG EEFDIPVLHL AQLLGLAMGL PKEDLVVDAH QVCVDECLEK LEELDRLAPG
SG