ID   HDRB_METMA              Reviewed;         300 AA.
AC   Q8PY83;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit B {ECO:0000250|UniProtKB:Q8TLB2};
DE            EC=1.8.7.3 {ECO:0000250|UniProtKB:Q8TLB2};
GN   Name=hdrB; OrderedLocusNames=MM_0980;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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:Q8TLB2}.
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:0000250|UniProtKB:Q8TLB2};
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:0000250|UniProtKB:Q8TLB2}.
CC   -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC       of three subunits; HdrA, HdrB and HdrC. {ECO:0000250|UniProtKB:Q8TLB2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TLB2}.
CC   -!- SIMILARITY: Belongs to the HdrB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM30676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM30676.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048041296.1; NC_003901.1.
DR   AlphaFoldDB; Q8PY83; -.
DR   SMR; Q8PY83; -.
DR   STRING; 192952.MM_0980; -.
DR   EnsemblBacteria; AAM30676; AAM30676; MM_0980.
DR   GeneID; 24876465; -.
DR   KEGG; mma:MM_0980; -.
DR   PATRIC; fig|192952.21.peg.1155; -.
DR   eggNOG; arCOG00338; Archaea.
DR   HOGENOM; CLU_052147_1_0_2; -.
DR   OMA; PGCVAQG; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000000595; 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:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Ferredoxin:CoB-CoM heterodisulfide reductase subunit
FT                   B"
FT                   /id="PRO_0000150068"
SQ   SEQUENCE   300 AA;  33068 MW;  B694E9152DE0A3DE CRC64;
     MNKLSLFLGC IVPNRYPGIE KATKLCLQRL EIDACDLPGA SCCPAPGVFK SFDKATWLAL
     ASRNIVLSER MERDVLTVCN GCYGSLADAN MELKKDPEMK ACTNSCLKEI GMEFRGTSEI
     RHIIEFLYKE FGPEKLKEYI TTPLDLKVAL HYGCHLIKPS KDRNLGDTES PVFFDELVEA
     TGAKSVDYTD KMMCCGAGGG VRSGYADESL EMLEHKLDCI CKAGVDCIVN ACPFCHLQFD
     RGQIAVNEKF GTDYSIPVLH YSQLLGLALG FSPDQLGIEQ NAVQNIEFLA KIYEISAGLS