ID MCRG_METBF Reviewed; 248 AA. AC P07964; Q46E24; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 153. 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; OrderedLocusNames=Mbar_A0894; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3502709; DOI=10.1093/nar/15.10.4350; RA Bokranz M., Klein A.; RT "Nucleotide sequence of the methyl coenzyme M reductase gene cluster from RT Methanosarcina barkeri."; RL Nucleic Acids Res. 15:4350-4351(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/jb.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). RN [3] {ECO:0007744|PDB:1E6Y} RP PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN RP COMPLEX WITH COENZYME F430; COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA RP AND BETA, FUNCTION, COFACTOR, AND SUBUNIT. RC STRAIN=Fusaro / DSM 804; RX PubMed=11023796; DOI=10.1006/jmbi.2000.4136; RA Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.; RT "Comparison of three methyl-coenzyme M reductases from phylogenetically RT distant organisms: unusual amino acid modification, conservation and RT adaptation."; RL J. Mol. Biol. 303:329-344(2000). 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:0000305|PubMed:11023796}. 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:0000269|PubMed:11023796}; CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme CC F430 is a yellow nickel porphinoid (PubMed:11023796). Methyl-coenzyme-M CC reductase is activated when the enzyme-bound coenzyme F430 is reduced CC to the Ni(I) oxidation state (By similarity). CC {ECO:0000250|UniProtKB:P11562, ECO:0000269|PubMed:11023796}; 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:0000269|PubMed:11023796}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; Y00158; CAA68356.1; -; Genomic_DNA. DR EMBL; CP000099; AAZ69868.1; -; Genomic_DNA. DR PIR; D29525; D29525. DR PDB; 1E6Y; X-ray; 1.60 A; C/F=2-248. DR PDBsum; 1E6Y; -. DR AlphaFoldDB; P07964; -. DR SMR; P07964; -. DR STRING; 269797.Mbar_A0894; -. DR PaxDb; 269797-Mbar_A0894; -. DR GeneID; 24821496; -. DR KEGG; mba:Mbar_A0894; -. DR eggNOG; arCOG04858; Archaea. DR HOGENOM; CLU_1092436_0_0_2; -. DR OrthoDB; 52520at2157; -. DR BRENDA; 2.8.4.1; 3250. DR UniPathway; UPA00646; UER00699. DR EvolutionaryTrace; P07964; -. 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; Methyl-coenzyme M reductase, gamma subunit; 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 NCBIfam; TIGR03259; met_CoM_red_gam; 1. DR Pfam; PF02240; MCR_gamma; 1. DR PIRSF; PIRSF000264; Meth_CoM_rd_gama; 1. DR SUPFAM; SSF55088; Methyl-coenzyme M reductase subunits; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Methanogenesis; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..248 FT /note="Methyl-coenzyme M reductase subunit gamma" FT /id="PRO_0000147473" FT BINDING 121 FT /ligand="coenzyme M" FT /ligand_id="ChEBI:CHEBI:58319" FT /evidence="ECO:0000269|PubMed:11023796, FT ECO:0007744|PDB:1E6Y" FT HELIX 13..23 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 34..41 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 66..70 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 75..79 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:1E6Y" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 99..109 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 128..140 FT /evidence="ECO:0007829|PDB:1E6Y" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:1E6Y" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 206..212 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:1E6Y" FT HELIX 227..245 FT /evidence="ECO:0007829|PDB:1E6Y" SQ SEQUENCE 248 AA; 27811 MW; AB23870B4BD7160B CRC64; MAYERQYYPG ATSVAANRRK HMSGKLEKLR EISDEDLTAV LGHRAPGSDY PSTHPPLAEM GEPACSTREN VAATPGAAAG DRVRYIQFAD SMYNAPATPY FRSYFAAINF RGVDPGTLSG RQIVEARERD MEQCAKVQME TEITDHALAG VRGATVHGHS VRLQEDGVMF DMLDRRRLEN GTIIMDKDQV AIPLDRKVDL GKPMSSEEAA KRTTIYRVDN VAFRDDAEVV EWVHRIFDQR TKFGFQPK //