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 16-JUN-2009, entry version 57. 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 (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=2190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX MEDLINE=96337999; 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 an heterodisulfide (By similarity). CC -!- CATALYTIC ACTIVITY: 2-(methylthio)ethanesulfonate (methyl-CoM) + CC N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = CoM- CC 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-CoM reduction; methane from CC methyl-CoM: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains (By CC similarity). 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; L77117; AAB98850.1; -; Genomic_DNA. DR PIR; E64405; E64405. DR RefSeq; NP_247839.1; -. DR HSSP; Q49604; 1E6V. DR GeneID; 1451733; -. DR GenomeReviews; L77117_GR; MJ0845. DR KEGG; mja:MJ0845; -. DR NMPDR; fig|243232.1.peg.876; -. DR TIGR; MJ0845; -. DR HOGENOM; Q58255; -. DR OMA; Q58255; GAKEGHR. DR BioCyc; MJAN243232:MJ_0845-MON; -. DR BRENDA; 2.8.4.1; 256362. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:EC. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR003178; Me_CoM_Rdtase_gsu. DR Gene3D; G3DSA:3.90.320.20; MCR_gamma; 1. DR Pfam; PF02240; MCR_gamma; 1. DR PIRSF; PIRSF000264; Meth_CoM_rd_gama; 1. DR ProDom; PD005845; MCR_gamma; 1. DR TIGRFAMs; TIGR03259; met_CoM_red_gam; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; 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 //