ID Q49601_9EURY Unreviewed; 444 AA.
AC Q49601; Q7LWW5;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 120.
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:AAB01999.1};
GN ORFNames=HA336_02680 {ECO:0000313|EMBL:HII70124.1};
OS Methanopyrus kandleri.
OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC Methanopyraceae; Methanopyrus.
OX NCBI_TaxID=2320 {ECO:0000313|EMBL:AAB01999.1};
RN [1] {ECO:0000313|EMBL:AAB01999.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8863453;
RA Nolling J., Elfner A., Palmer J.R., Steigerwald V.J., Pihl T.D., Lake J.A.,
RA Reeve J.N.;
RT "Phylogeny of Methanopyrus kandleri based on methyl coenzyme M reductase
RT operons.";
RL Int. J. Syst. Bacteriol. 46:1170-1173(1996).
RN [2] {ECO:0007829|PDB:1E6V}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH COENZYME B.
RX PubMed=11023796; DOI=10.1006/jmbi.2000.4136;
RA Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.;
RT "Comparison of three methyl-coenzyme M reductases from phylogenetically
RT distant organisms: unusual amino acid modification, conservation and
RT adaptation.";
RL J. Mol. Biol. 303:329-344(2000).
RN [3] {ECO:0000313|EMBL:HII70124.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UBA8853 {ECO:0000313|EMBL:HII70124.1};
RX DOI=10.1101/2020.03.01.972265;
RA Rinke C., Chuvochina M., Mussig A.J., Chaumeil P.-A., Waite D.W.,
RA Whitman W.B., Parks D.H., Hugenholtz P.;
RT "A rank-normalized archaeal taxonomy based on genome phylogeny resolves
RT widespread incomplete and uneven classifications.";
RL bioRxiv 0:0-0(2020).
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; U57340; AAB01999.1; -; Genomic_DNA.
DR EMBL; DUJS01000002; HII70124.1; -; Genomic_DNA.
DR PDB; 1E6V; X-ray; 2.70 A; B/E=1-444.
DR PDBsum; 1E6V; -.
DR OMA; TAMFEMG; -.
DR BRENDA; 2.8.4.1; 3274.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000619545; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1E6V};
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994,
KW ECO:0000256|PIRNR:PIRNR000263};
KW Transferase {ECO:0000256|PIRNR:PIRNR000263, ECO:0000313|EMBL:HII70124.1}.
FT DOMAIN 7..188
FT /note="Methyl-coenzyme M reductase beta subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02783"
FT DOMAIN 190..438
FT /note="Methyl-coenzyme M reductase beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02241"
SQ SEQUENCE 444 AA; 48241 MW; A3DECC20A50E097C CRC64;
MAREAKDTVD LYDDRGNCVA EEVPIEVLSP MRNEAIQSIV NDIKRTVAID LEGIENALQN
ATVGGKGMKI PGREMDVDIV DNAEAIADEI EKMIRVYEDD DTNVEPMYDG KRLLVQLPSE
RVKVMADPYS GTLQAGMAVV HAIIDVCEVD MWDANMVKAA VFGRYPQTID YFGGNVASML
DVPMKQEGVG YALRNIMVNH IVAATRKNTM QAVCLAATLE QTAMFEMGDA LGPFERLHLL
GYAYQGLNAD NMVYDIVKKH GKEGTVGTVV REVVERALED GVIEVKEELP SGFKVYKAND
MDLWNAYAAA GLVAAVMVNQ GAARAAQGVS ATILYYNDLL EYETGLPGVD FGRAEGTAVG
FSFFSHSIYG GGGPGIFHGN HIVTRHSKGF AIPPVAAAMA LDAGTQMFSP EVTSKLIGDV
FGEIDEFREP MKYITEAAAE EAKR
//
