ID Q2NI03_METST Unreviewed; 442 AA.
AC Q2NI03;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=mrtB {ECO:0000313|EMBL:ABC56728.1};
GN OrderedLocusNames=Msp_0318 {ECO:0000313|EMBL:ABC56728.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC56728.1, ECO:0000313|Proteomes:UP000001931};
RN [1] {ECO:0000313|EMBL:ABC56728.1, ECO:0000313|Proteomes:UP000001931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC {ECO:0000313|Proteomes:UP000001931};
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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 -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00010675}.
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DR EMBL; CP000102; ABC56728.1; -; Genomic_DNA.
DR RefSeq; WP_011405928.1; NC_007681.1.
DR AlphaFoldDB; Q2NI03; -.
DR SMR; Q2NI03; -.
DR STRING; 339860.Msp_0318; -.
DR GeneID; 41324891; -.
DR KEGG; mst:Msp_0318; -.
DR eggNOG; arCOG04860; Archaea.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OrthoDB; 52873at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000001931; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000001931};
KW Transferase {ECO:0000256|PIRNR:PIRNR000263, ECO:0000313|EMBL:ABC56728.1}.
FT DOMAIN 6..186
FT /note="Methyl-coenzyme M reductase beta subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02783"
FT DOMAIN 188..435
FT /note="Methyl-coenzyme M reductase beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02241"
SQ SEQUENCE 442 AA; 46707 MW; 791549D244CB6450 CRC64;
MPTYEDKIDL YGVDGKLLEE QVPLEAISPV INPTIKNIIQ EIKRSVAINL AGIEKSLANG
AYGGKANFIP GRELELDIVD NADAIADKIE KMLKISDDDD FNLNLLNGGK QILVQVPSER
LSIAGDYSVA PLATGSALIQ AILDTFDINK YQASEIKTAA MGGYPHNVKL GGALTTLLGQ
TTHLEGLGYS LRNIGANHVV AITKKNTLNA VALSSILEQT ATFEMGDAVG AFERSHLLGL
AYQGLNANNI VYDLVKENGK ATLGDVIISL LSRALDDGVI RVKETLPSGF KLYEPVDWAL
WNAYAAAGLI AATIVNVGAA RAAQGVASSI LYFNDILEYE AGLPGVDFGR VMGTGVGMSF
FSHGIYGGGG PGVFNGNHVV TRHSKGYAIP CNAAAMALDA GTQMFSVEST SGLVGEVYGS
VDNLREPVKY VAEGASQVKD KL
//
