ID   MCRG_METJA              Reviewed;         260 AA.
AC   Q58255;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Methyl-coenzyme M reductase I subunit gamma;
DE            Short=MCR I gamma;
DE            EC=2.8.4.1 {ECO:0000250|UniProtKB:P11562};
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma;
GN   Name=mcrG; OrderedLocusNames=MJ0845;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98850.1; -; Genomic_DNA.
DR   PIR; E64405; E64405.
DR   RefSeq; WP_010870359.1; NC_000909.1.
DR   AlphaFoldDB; Q58255; -.
DR   SMR; Q58255; -.
DR   STRING; 243232.MJ_0845; -.
DR   PRIDE; Q58255; -.
DR   EnsemblBacteria; AAB98850; AAB98850; MJ_0845.
DR   GeneID; 1451733; -.
DR   KEGG; mja:MJ_0845; -.
DR   eggNOG; arCOG04858; Archaea.
DR   HOGENOM; CLU_1092436_0_0_2; -.
DR   InParanoid; Q58255; -.
DR   OMA; IMGHRQP; -.
DR   OrthoDB; 51032at2157; -.
DR   PhylomeDB; Q58255; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000000805; 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   3: Inferred from homology;
KW   Cytoplasm; Methanogenesis; Reference proteome; Transferase.
FT   CHAIN           1..260
FT                   /note="Methyl-coenzyme M reductase I subunit gamma"
FT                   /id="PRO_0000147476"
FT   BINDING         123
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P11562"
SQ   SEQUENCE   260 AA;  30174 MW;  34413840D8EADACE CRC64;
     MAYKPQFYPG QTKIAQNRRD HMNPDVQLEK LRDIPDDDVV KIMGHRQPGE DYKTVHPPLE
     EMDLPEDYVR DLVEPLNGAK EGHRIRYIQF TDSMYFAPAQ PYDRARTYMW RFRGVDTGTL
     SGRQVIEMRE SDLEALSKNF LIDTAFFDPA RIGIRGATVH GHSLRLDENG LMFDALQRYV
     YDEKTGHVLY VKDQVGRPLD EPVDVGEPLP EEKLKEITTI YRIDGVPMRE DEELLTVVKR
     IHRARTLGGF LPVEDVFEKL