MCRG_METTH
ID MCRG_METTH Reviewed; 249 AA.
AC O27233; Q50492;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Methyl-coenzyme M reductase I subunit gamma {ECO:0000303|PubMed:2269306};
DE Short=MCR I gamma {ECO:0000303|PubMed:2269306};
DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3122735};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma;
GN Name=mcrG; OrderedLocusNames=MTH_1165;
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:P11562};
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:P11562};
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:P11562}.
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:P11562}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85654.1; 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; AAA73444.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85654.1; ALT_INIT; Genomic_DNA.
DR PIR; C69022; C69022.
DR RefSeq; WP_048060982.1; NC_000916.1.
DR AlphaFoldDB; O27233; -.
DR SMR; O27233; -.
DR IntAct; O27233; 1.
DR STRING; 187420.MTH_1165; -.
DR EnsemblBacteria; AAB85654; AAB85654; MTH_1165.
DR GeneID; 1471573; -.
DR KEGG; mth:MTH_1165; -.
DR PATRIC; fig|187420.15.peg.1142; -.
DR HOGENOM; CLU_1092436_0_0_2; -.
DR OMA; IMGHRQP; -.
DR BioCyc; MetaCyc:MCRGMAUTO-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 CDD; cd00539; MCR_gamma; 1.
DR Gene3D; 3.90.320.20; -; 1.
DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold.
DR InterPro; IPR003178; Me_CoM_Rdtase_gsu.
DR InterPro; IPR036994; Me_CoM_Rdtase_gsu_sf.
DR Pfam; PF02240; MCR_gamma; 1.
DR PIRSF; PIRSF000264; Meth_CoM_rd_gama; 1.
DR SUPFAM; SSF55088; SSF55088; 1.
DR TIGRFAMs; TIGR03259; met_CoM_red_gam; 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..249
FT /note="Methyl-coenzyme M reductase I subunit gamma"
FT /id="PRO_0000147478"
FT BINDING 120
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11562"
SQ SEQUENCE 249 AA; 28717 MW; 95C9C36D111BA5C6 CRC64;
MAQYYPGTSK VAQNRRNFCN PEYELEKLRE ISDEDVVKIL GHRAPGEEYP SVHPPLEEMD
EPEDAIREMV EPIDGAKAGD RVRYIQFTDS MYFAPAQPYV RSRAYLCRYR GADAGTLSGR
QIIETRERDL EKISKELLET EFFDPARSGV RGKSVHGHSL RLDEDGMMFD MLRRQIYNKD
TGRVEMVKNQ IGDELDEPVD LGEPLDEETL MNKTTIYRVD GEAYRDDTDA VEIMQRIHVL
RSQGGYNPE
