MCRB_METTH
ID MCRB_METTH Reviewed; 443 AA.
AC O27236; Q50489;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Methyl-coenzyme M reductase I subunit beta {ECO:0000303|PubMed:2269306};
DE Short=MCR I beta {ECO:0000303|PubMed:2269306};
DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3122735};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta;
GN Name=mcrB; OrderedLocusNames=MTH_1168;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=7929010; DOI=10.1128/jb.176.20.6384-6391.1994;
RA Pihl T.D., Sharma S., Reeve J.N.;
RT "Growth phase-dependent transcription of the genes that encode the two
RT methyl coenzyme M reductase isoenzymes and N5-
RT methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT Methanobacterium thermoautotrophicum delta H.";
RL J. Bacteriol. 176:6384-6391(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=2269306; DOI=10.1111/j.1432-1033.1990.tb19481.x;
RA Rospert S., Linder D., Ellermann J., Thauer R.K.;
RT "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium
RT thermoautotrophicum strain Marburg and delta H.";
RL Eur. J. Biochem. 194:871-877(1990).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=3122735; DOI=10.1016/0006-291x(87)90389-5;
RA Bobik T.A., Olson K.D., Noll K.M., Wolfe R.S.;
RT "Evidence that the heterodisulfide of coenzyme M and 7-
RT mercaptoheptanoylthreonine phosphate is a product of the methylreductase
RT reaction in Methanobacterium.";
RL Biochem. Biophys. Res. Commun. 149:455-460(1987).
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:0000269|PubMed:2269306, ECO:0000269|PubMed:3122735}.
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:0000269|PubMed:2269306, ECO:0000269|PubMed:3122735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000305|PubMed:2269306};
CC -!- COFACTOR:
CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC Evidence={ECO:0000250|UniProtKB:P11560};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is
CC activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I)
CC oxidation state. {ECO:0000250|UniProtKB:P11560};
CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC from methyl-coenzyme M: step 1/1. {ECO:0000305|PubMed:2269306}.
CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC forming a dimer of heterotrimers. {ECO:0000269|PubMed:2269306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11560}.
CC -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria. MCR
CC II is expressed in the early growth phase. Late growth cells contain
CC mostly MCR I. {ECO:0000250|UniProtKB:P11560}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase beta subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U10036; AAA73441.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85657.1; ALT_INIT; Genomic_DNA.
DR PIR; F69022; F69022.
DR RefSeq; WP_048061283.1; NC_000916.1.
DR AlphaFoldDB; O27236; -.
DR SMR; O27236; -.
DR IntAct; O27236; 1.
DR STRING; 187420.MTH_1168; -.
DR EnsemblBacteria; AAB85657; AAB85657; MTH_1168.
DR GeneID; 1471576; -.
DR KEGG; mth:MTH_1168; -.
DR PATRIC; fig|187420.15.peg.1145; -.
DR HOGENOM; CLU_617682_0_0_2; -.
DR OMA; TAMFEMG; -.
DR BioCyc; MetaCyc:MCRBMAUTO-MON; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.840.10; -; 1.
DR Gene3D; 3.30.70.470; -; 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 Pfam; PF02241; MCR_beta; 1.
DR Pfam; PF02783; MCR_beta_N; 1.
DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1.
DR SUPFAM; SSF48081; SSF48081; 1.
DR SUPFAM; SSF55088; SSF55088; 1.
DR TIGRFAMs; TIGR03257; met_CoM_red_bet; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Methanogenesis; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2269306"
FT CHAIN 2..443
FT /note="Methyl-coenzyme M reductase I subunit beta"
FT /id="PRO_0000147467"
FT BINDING 367
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11560"
FT BINDING 369
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000250|UniProtKB:P11560"
FT CONFLICT 82
FT /note="A -> C (in Ref. 1; AAA73441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 47224 MW; 132DFCD54BBB734E CRC64;
MAKFEDKVDL YDDRGNLVEE QVPLEALSPL RNPAIKSIVQ GIKRTVAVNL EGIENALKTA
KVGGPACKIM GRELDLDIVG NAESIAAAAK EMIQVTEDDD TKVELLGGGK RALVQVPSAR
FDVAAEYSAA PLVTATAFVQ AIINEFDVSM YDANMVKAAV LGRYPQSVEY MGANIATMLD
IPQKLEGPGY ALRNIMVNHV VAATLKNTLQ AAALSTILEQ TAMFEMGDAV GAFERMHLLG
LAYQGMNADN LVFDLVKANG KEGTVGSVIA DLVERALEDG VIKVEKELTD YKVYGTDDLA
MWNAYAAAGL MAATMVNQGA ARAAQGVSST LLYYNDLIEF ETGLPGVDFG KVEGTAVGFS
FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD AGTQMFSPEA TSGLIKEVFS
QVDEFREPLK YVVEAAAEIK NEI
