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Database: UniProt
Entry: A6UQK1_METVS
LinkDB: A6UQK1_METVS
Original site: A6UQK1_METVS 
ID   A6UQK1_METVS            Unreviewed;       443 AA.
AC   A6UQK1;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Methyl-coenzyme M reductase subunit beta {ECO:0000256|PIRNR:PIRNR000263};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000263};
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase beta {ECO:0000256|PIRNR:PIRNR000263};
GN   OrderedLocusNames=Mevan_0868 {ECO:0000313|EMBL:ABR54773.1};
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327 {ECO:0000313|EMBL:ABR54773.1, ECO:0000313|Proteomes:UP000001107};
RN   [1] {ECO:0000313|EMBL:ABR54773.1, ECO:0000313|Proteomes:UP000001107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB
RC   {ECO:0000313|Proteomes:UP000001107};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that
CC       catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-
CC       (methylthio)ethanesulfonate) using coenzyme B (CoB or 7-
CC       mercaptoheptanoylthreonine phosphate) as reductant which results in the
CC       production of methane and the mixed heterodisulfide of CoB and CoM
CC       (CoM-S-S-CoB). This is the final step in methanogenesis.
CC       {ECO:0000256|ARBA:ARBA00002461}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B
CC         heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183,
CC         ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000951};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC         Evidence={ECO:0000256|ARBA:ARBA00000951};
CC   -!- COFACTOR:
CC       Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001952};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC       from methyl-coenzyme M: step 1/1. {ECO:0000256|ARBA:ARBA00005149,
CC       ECO:0000256|PIRNR:PIRNR000263}.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC       {ECO:0000256|PIRNR:PIRNR000263}.
CC   -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC       forming a dimer of heterotrimers. {ECO:0000256|ARBA:ARBA00011155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC       family. {ECO:0000256|ARBA:ARBA00010675}.
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DR   EMBL; CP000742; ABR54773.1; -; Genomic_DNA.
DR   RefSeq; WP_011972674.1; NC_009634.1.
DR   AlphaFoldDB; A6UQK1; -.
DR   STRING; 406327.Mevan_0868; -.
DR   GeneID; 5326167; -.
DR   KEGG; mvn:Mevan_0868; -.
DR   eggNOG; arCOG04860; Archaea.
DR   HOGENOM; CLU_617682_0_0_2; -.
DR   OMA; TAMFEMG; -.
DR   OrthoDB; 52873at2157; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000001107; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.470; -; 1.
DR   Gene3D; 1.20.840.10; Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal; 1.
DR   InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C.
DR   InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2.
DR   InterPro; IPR003179; Me_CoM_Rdtase_bsu.
DR   InterPro; IPR022679; Me_CoM_Rdtase_bsu_C.
DR   InterPro; IPR022680; Me_CoM_Rdtase_bsu_N.
DR   InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold.
DR   NCBIfam; TIGR03257; met_CoM_red_bet; 1.
DR   Pfam; PF02241; MCR_beta; 1.
DR   Pfam; PF02783; MCR_beta_N; 1.
DR   PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1.
DR   SUPFAM; SSF48081; Methyl-coenzyme M reductase alpha and beta chain C-terminal domain; 1.
DR   SUPFAM; SSF55088; Methyl-coenzyme M reductase subunits; 1.
PE   3: Inferred from homology;
KW   Methanogenesis {ECO:0000256|ARBA:ARBA00022994,
KW   ECO:0000256|PIRNR:PIRNR000263};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000263, ECO:0000313|EMBL:ABR54773.1}.
FT   DOMAIN          6..187
FT                   /note="Methyl-coenzyme M reductase beta subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02783"
FT   DOMAIN          189..436
FT                   /note="Methyl-coenzyme M reductase beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02241"
SQ   SEQUENCE   443 AA;  46896 MW;  19CBD244D89BD8B4 CRC64;
     MVKYEDKISL YDAKGNLVAE NVPLEAISPL YNPTIKSMLK NIKRTVAVNL AGIENTLATG
     SIGGKGCKVP GRTLDLSVVS NAQAIADEVE KILKVSKDDD TAIKLINGGK QMAVQVPSER
     LEVAAEYSVS MLATAMALKE AIIKTFNVDM FEGSTVHASI MGNYPQVMDY AGGNIASLLG
     APSNLEGLGY ALRNIPVNHA VATTKKNMMN AIAFSSVMEQ TATFEMGDAI GSFERQHLLG
     LAYQGLNADN LVIEFIKANG KGTVGTVVQS VVERALADGV IVVDKTMGSG FNMYKPADVN
     KWNAYAAAGL VAAAAVSCGA ARAAQNIASV ILYYNDILEY ETGLPGVDYG RSMGTAVGFS
     FFSHSIYGGG GPGIFNGNHV VTRHSKGFAI PPVCAAMCAD AGTQMFSPEH TSALVGAVYS
     AFDEFREPMK YVIERALNIK DKL
//
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