ID   MCRG_METVO              Reviewed;         261 AA.
AC   P11563;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Methyl-coenzyme M reductase subunit gamma;
DE            EC=2.8.4.1 {ECO:0000250|UniProtKB:P11562};
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma;
GN   Name=mcrG;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=3185509; DOI=10.1007/bf00339610;
RA   Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.;
RT   "Comparative analysis of genes encoding methyl coenzyme M reductase in
RT   methanogenic bacteria.";
RL   Mol. Gen. Genet. 213:409-420(1988).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11562}.
CC   -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit
CC       family. {ECO:0000305}.
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DR   EMBL; X07793; CAA30632.1; -; Genomic_DNA.
DR   PIR; S03260; S03260.
DR   AlphaFoldDB; P11563; -.
DR   SMR; P11563; -.
DR   UniPathway; UPA00646; UER00699.
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; 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   Cytoplasm; Methanogenesis; Transferase.
FT   CHAIN           1..261
FT                   /note="Methyl-coenzyme M reductase subunit gamma"
FT                   /id="PRO_0000147484"
FT   BINDING         123
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P11562"
SQ   SEQUENCE   261 AA;  30132 MW;  236BA6C71F5AAA49 CRC64;
     MAYKPQFYPS ATKVAENRRN HINPAFELEK LREIPDEDVV KIMGHRQPSE DYKTVHPPLE
     EMDLAEDYVR DLVGPINGAK EGHRIRYIQF ADSMYFAPSQ PYDRSRLYMS RFRGVDCGTL
     SGRQVVELRE SNLEDISKNY LVDTELFDPA TTGMRGATVH GHSLRLDENG VMFDALQRYE
     FDEATGHILY VKDQVGRPWD EPVDVGEPVP QEKLKEITTI YRKDGVAMRD DMEVVEVVKR
     IHRARTLGGY CPLNEIFDTY L