ID   HDRB1_METAC             Reviewed;         314 AA.
AC   Q8TLB2;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit B {ECO:0000305};
DE            EC=1.8.7.3 {ECO:0000305|PubMed:19968794};
GN   Name=hdrB1 {ECO:0000303|PubMed:19968794};
GN   OrderedLocusNames=MA_3126 {ECO:0000312|EMBL:AAM06499.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=19968794; DOI=10.1111/j.1365-2958.2009.06990.x;
RA   Buan N.R., Metcalf W.W.;
RT   "Methanogenesis by Methanosarcina acetivorans involves two structurally and
RT   functionally distinct classes of heterodisulfide reductase.";
RL   Mol. Microbiol. 75:843-853(2010).
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). Probably involved in methylotrophic methanogenesis but
CC       not in aceticlastic methanogenesis. {ECO:0000269|PubMed:19968794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC         coenzyme M-coenzyme B heterodisulfide + 2 H(+) + 2 reduced [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:55160, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.7.3;
CC         Evidence={ECO:0000305|PubMed:19968794};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q8TIB8};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q8TIB8};
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 ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC       of three subunits; HdrA1, HdrB1 and HdrC1.
CC       {ECO:0000269|PubMed:19968794}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Induced on trimethylamine or methanol, but not on acetate as
CC       the sole energy source. {ECO:0000269|PubMed:19968794}.
CC   -!- DISRUPTION PHENOTYPE: Triple hdrA1C1B1 deletion decreases methane
CC       production from methanol, but does not affect methanogenesis from
CC       acetate. Deletion results in up-regulation of CoB-SH and CoM-SH
CC       synthesis and transport, and methylsulfide methyltransferases.
CC       {ECO:0000269|PubMed:19968794}.
CC   -!- SIMILARITY: Belongs to the HdrB family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM06499.1; -; Genomic_DNA.
DR   RefSeq; WP_011023064.1; NC_003552.1.
DR   AlphaFoldDB; Q8TLB2; -.
DR   SMR; Q8TLB2; -.
DR   STRING; 188937.MA_3126; -.
DR   EnsemblBacteria; AAM06499; AAM06499; MA_3126.
DR   GeneID; 1475020; -.
DR   KEGG; mac:MA_3126; -.
DR   HOGENOM; CLU_052147_0_0_2; -.
DR   OMA; YPERRHC; -.
DR   OrthoDB; 73750at2157; -.
DR   PhylomeDB; Q8TLB2; -.
DR   BioCyc; MetaCyc:MON-20157; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   Pfam; PF02754; CCG; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..314
FT                   /note="Ferredoxin:CoB-CoM heterodisulfide reductase subunit
FT                   B"
FT                   /id="PRO_0000443935"
SQ   SEQUENCE   314 AA;  35327 MW;  0EAD3114C8064107 CRC64;
     MKAIESIPDR KLLLFKSCMV GQEYPGIETA TSYVFDRLGV DYCINDEQSC CTGIGHYTDV
     FEGLTTAAIA ARNFAVARKC GYPNITCLCS TCYAINKDAC ELLNTNDGVR EKVNSIFREK
     GFDDLVYEKD SMNPRTNIYH AVEVLLSKVE KIREEIKFDF PGVKAASHHA CHYYKVKYLD
     VIGNPENPQL IDTIAEACGA SPVRWYEDRT LTCGMGFSQL HLNKSTSLQV TKTKLDSLQR
     AGVELMIHMC PNCHIQYDRY QPVIEKEFGV EYDMVHMNIA QFVALSMGAD PYKVCGFQTH
     SVPLEGFLEK TGII