ID Q2FSD8_METHJ Unreviewed; 435 AA.
AC Q2FSD8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Mhun_2144 {ECO:0000313|EMBL:ABD41850.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD41850.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD41850.1; -; Genomic_DNA.
DR RefSeq; WP_011449108.1; NC_007796.1.
DR AlphaFoldDB; Q2FSD8; -.
DR SMR; Q2FSD8; -.
DR STRING; 323259.Mhun_2144; -.
DR EnsemblBacteria; ABD41850; ABD41850; Mhun_2144.
DR GeneID; 3922301; -.
DR KEGG; mhu:Mhun_2144; -.
DR eggNOG; arCOG04860; Archaea.
DR HOGENOM; CLU_617682_0_0_2; -.
DR InParanoid; Q2FSD8; -.
DR OrthoDB; 52873at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000001941; 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:UP000001941};
KW Transferase {ECO:0000256|PIRNR:PIRNR000263, ECO:0000313|EMBL:ABD41850.1}.
FT DOMAIN 6..185
FT /note="Methyl-coenzyme M reductase beta subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02783"
FT DOMAIN 187..435
FT /note="Methyl-coenzyme M reductase beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02241"
SQ SEQUENCE 435 AA; 45893 MW; E98F2BC0DEA872F0 CRC64;
MAKFSDTIDL YDDQGKLLKS GVALDKVSPL TNAGIKKMIS LTKRTVAVNL GGAEAFLKTG
KAGKNQIPGR ELNLDLVANA GAIKEKMFKM LQVTEGDDTE IKEFGGGKLL LCTVPTARIE
AAATYDAAMT AVSAAATYAV IDQFNVDMFN GSTVKAAFWG TYPQTMDPSG SACASILSIP
QNNEGLGYAL RNIQANHCVM ITNKNAMQGA ALSATFEQAG EFEMGAAIGP FERAQLLLYA
YQGLNANNLV YDLVKKNGAT GTIGTVVQSL VERAIEDKVI TPGKKGPSGY IFYETKDPML
WNAYTAAGTM AATMVNCGAG RFAQAVSSTL LYFNDLIEHE TGLPGCDYGR VMGVAVGFSF
FSHSIYGGGG PGIFNGNHVV TRHAAGVGLP CIVAACALDA GTQMFSPEST SKVYQDTFGK
IPEFAQPIQH IAQGA
//
