MCRZ_METFV
ID MCRZ_METFV Reviewed; 267 AA.
AC Q49173; E3GZ00;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Methyl-coenzyme M reductase II subunit gamma;
DE Short=MCR II gamma;
DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11562};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma;
GN Name=mrtG; Synonyms=mcrIIG; OrderedLocusNames=Mfer_0733;
OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=523846;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=8177216; DOI=10.1007/bf00280317;
RA Lehmacher A., Klenk H.-P.;
RT "Characterization and phylogeny of mcrII, a gene cluster encoding an
RT isoenzyme of methyl coenzyme M reductase from hyperthermophilic
RT Methanothermus fervidus.";
RL Mol. Gen. Genet. 243:198-206(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=21304736; DOI=10.4056/sigs.1283367;
RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL Stand. Genomic Sci. 3:315-324(2010).
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:0000250|UniProtKB:P11562}.
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:0000250|UniProtKB:P11562};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000250|UniProtKB:P11562};
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:0000250|UniProtKB:P11562}.
CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC forming a dimer of heterotrimers. {ECO:0000250|UniProtKB:P11562}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit
CC family. {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; X70765; CAA50043.1; -; Genomic_DNA.
DR EMBL; CP002278; ADP77532.1; -; Genomic_DNA.
DR PIR; S43900; S43900.
DR RefSeq; WP_013413810.1; NC_014658.1.
DR AlphaFoldDB; Q49173; -.
DR SMR; Q49173; -.
DR STRING; 523846.Mfer_0733; -.
DR EnsemblBacteria; ADP77532; ADP77532; Mfer_0733.
DR GeneID; 9962463; -.
DR KEGG; mfv:Mfer_0733; -.
DR HOGENOM; CLU_1092436_0_0_2; -.
DR OMA; GHRNPGE; -.
DR OrthoDB; 51032at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000002315; Chromosome.
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 3: Inferred from homology;
KW Methanogenesis; Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="Methyl-coenzyme M reductase II subunit gamma"
FT /id="PRO_0000147475"
FT BINDING 123
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11562"
SQ SEQUENCE 267 AA; 30847 MW; 150D5FFAE6BC6F9D CRC64;
MAYEPQFNPG ETKIAENRRK HMNPNYELKK LREIADEDIV RVLGHRSPGE SFKTVHPPLE
EMDFEEDPMK DIVEPIEGAK QGTRIRYIQF ADSMYNAPAQ PYDRARTYMW RFRGVDTGTL
SGRQVIEMRE LDLEKVSKIL LETEIFDPAR CGIRGATVHG HSLRFDENGL MFDALQRYIY
DEDSGHVVYV KDQVGRPLDQ PVDMGEPLPE DELKEITTIY RKDNIGMRED EELLEVVNKI
HEARTIGGFG MEVFKKDLNK RLGGANE
