ID Q6LWZ9_METMP Unreviewed; 443 AA.
AC Q6LWZ9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
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 Name=mcrB {ECO:0000313|EMBL:CAF31111.1};
GN OrderedLocusNames=MMP1555 {ECO:0000313|EMBL:CAF31111.1};
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377 {ECO:0000313|Proteomes:UP000000590};
RN [1] {ECO:0000313|EMBL:CAF31111.1, ECO:0000313|Proteomes:UP000000590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL {ECO:0000313|Proteomes:UP000000590};
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., Soll 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).
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; BX950229; CAF31111.1; -; Genomic_DNA.
DR RefSeq; WP_011171499.1; NC_005791.1.
DR AlphaFoldDB; Q6LWZ9; -.
DR STRING; 267377.MMP1555; -.
DR EnsemblBacteria; CAF31111; CAF31111; MMP1555.
DR GeneID; 2761737; -.
DR KEGG; mmp:MMP1555; -.
DR PATRIC; fig|267377.15.peg.1593; -.
DR eggNOG; arCOG04860; Archaea.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OrthoDB; 52873at2157; -.
DR BRENDA; 2.8.4.1; 3262.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000000590; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994,
KW ECO:0000256|PIRNR:PIRNR000263};
KW Oxidoreductase {ECO:0000313|EMBL:CAF31111.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000590};
KW Transferase {ECO:0000256|PIRNR:PIRNR000263}.
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; 46646 MW; 093A7FAB770E5B39 CRC64;
MVKYEDKISL YDAKGNLVAE NVPLEAISPL YNPTIKSMVK NIKRTVAVNL AGIEGTLAAG
KIGGKGCQVP GRTLDISAVS NAQAIADEVE KILKVSEDDD TAVKIINGGK QLAVQVPTAR
LDVAAEYSVS MLSTAMALKE ALIKTFNIDM FDGSTVHAAI VGNYPQVMDY AGGNIASLLG
APSMMEGLGY ALRNIPVNHA VATTKKNMMN AIAFSSVMEQ TATFEMGDAV GSFERQHLLG
LAYQGLNADN LVIDFIKANA KGTVGSVVET VIDRAIADGV IVVDKTMSSG FNMYKPADVN
KWNAYAAAGL VAAVAVSCGA ARAAQNVASV ILYFNDILEY ETGLPGVDYG RSMGTAVGFS
FFSHSIYGGG GPGIFNGNHV VTRHSKGFAI PPVCAAMCAD AGTQMFSPEH TSGLVGSVYS
AFDEFREPMK YVIEGALSIK DQF
//
