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   01-MAY-2013, entry version 85.
DE   RecName: Full=Methyl-coenzyme M reductase I subunit gamma;
DE            Short=MCR I gamma;
DE            EC=2.8.4.1;
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma;
GN   Name=mcrG; OrderedLocusNames=MJ0845;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; 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.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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: Reduction of methyl-coenzyme M (2-(methylthio)
CC       ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate
CC       to methane and a heterodisulfide (By similarity).
CC   -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane.
CC   -!- COFACTOR: Binds 2 coenzyme F430 noncovalently per hexamer.
CC       Coenzyme F430 is a yellow nickel porphinoid (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction;
CC       methane from methyl-coenzyme M: step 1/1.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains (By
CC       similarity).
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DR   EMBL; L77117; AAB98850.1; -; Genomic_DNA.
DR   PIR; E64405; E64405.
DR   RefSeq; NP_247839.1; NC_000909.1.
DR   ProteinModelPortal; Q58255; -.
DR   SMR; Q58255; 6-250.
DR   STRING; 243232.MJ0845; -.
DR   EnsemblBacteria; AAB98850; AAB98850; MJ_0845.
DR   GeneID; 1451733; -.
DR   KEGG; mja:MJ_0845; -.
DR   eggNOG; COG4057; -.
DR   KO; K00402; -.
DR   OMA; GAKEGHR; -.
DR   ProtClustDB; CLSK876060; -.
DR   UniPathway; UPA00646; UER00699.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA: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   Pfam; PF02240; MCR_gamma; 1.
DR   PIRSF; PIRSF000264; Meth_CoM_rd_gama; 1.
DR   ProDom; PD005845; Me_CoM_Rdtase_gsu; 1.
DR   SUPFAM; SSF55088; MCR_fer_like; 1.
DR   TIGRFAMs; TIGR03259; met_CoM_red_gam; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Methanogenesis; Reference proteome; Transferase.
FT   CHAIN         1    260       Methyl-coenzyme M reductase I subunit
FT                                gamma.
FT                                /FTId=PRO_0000147476.
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
//