ID MCRG_METTM Reviewed; 249 AA. AC P11562; D9PY30; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 143. DE RecName: Full=Methyl-coenzyme M reductase I subunit gamma {ECO:0000303|PubMed:2269306}; DE Short=MCR I gamma {ECO:0000303|PubMed:2269306}; DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma; GN Name=mcrG; OrderedLocusNames=MTBMA_c15490; OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium OS thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=2448287; DOI=10.1128/jb.170.2.568-577.1988; RA Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.; RT "Cloning and characterization of the methyl coenzyme M reductase genes from RT Methanobacterium thermoautotrophicum."; RL J. Bacteriol. 170:568-577(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=20802048; DOI=10.1128/jb.00844-10; RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., RA Gottschalk G., Thauer R.K.; RT "Complete genome sequence of Methanothermobacter marburgensis, a RT methanoarchaeon model organism."; RL J. Bacteriol. 192:5850-5851(2010). RN [3] RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND RP DEVELOPMENTAL STAGE. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=2269306; DOI=10.1111/j.1432-1033.1990.tb19481.x; RA Rospert S., Linder D., Ellermann J., Thauer R.K.; RT "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium RT thermoautotrophicum strain Marburg and delta H."; RL Eur. J. Biochem. 194:871-877(1990). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY RP REGULATION, PATHWAY, AND SUBUNIT. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=3350018; DOI=10.1111/j.1432-1033.1988.tb13941.x; RA Ellermann J., Hedderich R., Boecher R., Thauer R.K.; RT "The final step in methane formation. Investigations with highly purified RT methyl-CoM reductase (component C) from Methanobacterium RT thermoautotrophicum (strain Marburg)."; RL Eur. J. Biochem. 172:669-677(1988). RN [5] RP COFACTOR. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=9030728; DOI=10.1111/j.1432-1033.1997.00110.x; RA Goubeaud M., Schreiner G., Thauer R.K.; RT "Purified methyl-coenzyme-M reductase is activated when the enzyme-bound RT coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) RT citrate."; RL Eur. J. Biochem. 243:110-114(1997). RN [6] RP SUBCELLULAR LOCATION. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=23533332; DOI=10.1155/2013/920241; RA Wrede C., Walbaum U., Ducki A., Heieren I., Hoppert M.; RT "Localization of methyl-Coenzyme M reductase as metabolic marker for RT diverse methanogenic Archaea."; RL Archaea 2013:920241-920241(2013). RN [7] RP CATALYTIC ACTIVITY, AND REACTION MECHANISM. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=25691570; DOI=10.1074/jbc.m115.636761; RA Wongnate T., Ragsdale S.W.; RT "The reaction mechanism of methyl-coenzyme M reductase: how an enzyme RT enforces strict binding order."; RL J. Biol. Chem. 290:9322-9334(2015). RN [8] {ECO:0007744|PDB:1MRO} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-248 IN COMPLEX WITH COENZYME RP F430; COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND BETA, COFACTOR, AND RP SUBUNIT. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=9367957; DOI=10.1126/science.278.5342.1457; RA Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.; RT "Crystal structure of methyl-coenzyme M reductase: the key enzyme of RT biological methane formation."; RL Science 278:1457-1462(1997). RN [9] {ECO:0007744|PDB:1HBM, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1HBO, ECO:0007744|PDB:1HBU} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-249 IN COMPLEXES WITH RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M AND MCR SUBUNITS ALPHA RP AND BETA. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=11491299; DOI=10.1006/jmbi.2001.4647; RA Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., RA Lamzin V., Ermler U.; RT "On the mechanism of biological methane formation: structural evidence for RT conformational changes in methyl-coenzyme M reductase upon substrate RT binding."; RL J. Mol. Biol. 309:315-330(2001). RN [10] {ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3M2R, ECO:0007744|PDB:3M2U, ECO:0007744|PDB:3M2V, ECO:0007744|PDB:3M30, ECO:0007744|PDB:3M32} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-249 IN COMPLEXES WITH RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M; COENZYME B ANALOGS AND RP MCR SUBUNITS ALPHA AND BETA. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=20707311; DOI=10.1021/bi100458d; RA Cedervall P.E., Dey M., Pearson A.R., Ragsdale S.W., Wilmot C.M.; RT "Structural insight into methyl-coenzyme M reductase chemistry using RT coenzyme B analogues."; RL Biochemistry 49:7683-7693(2010). RN [11] {ECO:0007744|PDB:3POT} RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH COENZYME F430; RP COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND BETA. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=21438550; DOI=10.1021/ja110492p; RA Cedervall P.E., Dey M., Li X., Sarangi R., Hedman B., Ragsdale S.W., RA Wilmot C.M.; RT "Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase RT from Methanothermobacter marburgensis."; RL J. Am. Chem. Soc. 133:5626-5628(2011). RN [12] {ECO:0007744|PDB:5A0Y} RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH COENZYME F430; RP COENZYME B; COENZYME M AND MCR SUBUNITS ALPHA AND BETA. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=27467699; DOI=10.1002/anie.201603882; RA Wagner T., Kahnt J., Ermler U., Shima S.; RT "Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing RT Methane Formation."; RL Angew. Chem. Int. Ed. Engl. 55:10630-10633(2016). RN [13] {ECO:0007744|PDB:5G0R} RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH COENZYME B; COENZYME RP F430 AND MCR SUBUNITS ALPHA AND BETA, AND ACTIVITY REGULATION. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=27140643; DOI=10.1073/pnas.1600298113; RA Duin E.C., Wagner T., Shima S., Prakash D., Cronin B., Yanez-Ruiz D.R., RA Duval S., Rumbeli R., Stemmler R.T., Thauer R.K., Kindermann M.; RT "Mode of action uncovered for the specific reduction of methane emissions RT from ruminants by the small molecule 3-nitrooxypropanol."; RL Proc. Natl. Acad. Sci. U.S.A. 113:6172-6177(2016). 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 (PubMed:2269306, PubMed:3350018). Neither N-6-mercaptohexanoylthreonine CC phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H- CC SOcoTP) nor any other thiol compound such as CoA or CoM can substitute CC for CoB as the electron donor (PubMed:3350018). CC {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3350018}. 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:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, CC ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533; CC Evidence={ECO:0000269|PubMed:27140643, ECO:0000305|PubMed:3350018}; CC -!- COFACTOR: CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; CC Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, CC ECO:0000269|PubMed:9367957}; CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme CC F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). CC Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme CC F430 is reduced to the Ni(I) oxidation state (PubMed:9030728). CC {ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, CC ECO:0000269|PubMed:9367957}; CC -!- ACTIVITY REGULATION: Methyl-coenzyme M reductase activity is inhibited CC by 3-nitrooxypropanol (3-NOP) in vitro and in vivo, by oxidation of its CC active site Ni(I), which stops both growth and methanogenesis CC (PubMed:27140643). Is also inhibited by the reaction product CoM-S-S- CC CoB (PubMed:3350018). {ECO:0000269|PubMed:27140643, CC ECO:0000269|PubMed:3350018}. CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane CC from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643, CC ECO:0000269|PubMed:3350018}. CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains, CC forming a dimer of heterotrimers. {ECO:0000269|PubMed:2269306, CC ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9367957}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23533332}. CC Note=Under growth limiting conditions on nickel-depleted media, a CC fraction of 70% of the enzyme is localized close to the cytoplasmic CC membrane, which implies 'facultative' membrane association of the CC enzyme. {ECO:0000269|PubMed:23533332}. CC -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria. MCR CC II is expressed in the early growth phase. Late growth cells contain CC mostly MCR I. {ECO:0000269|PubMed:2269306}. CC -!- MISCELLANEOUS: The MCR reaction has been shown to follow an ordered bi- CC bi ternary complex mechanism, in which methyl-SCoM must enter the MCR CC active site prior to CoB for a productive catalysis. CC {ECO:0000269|PubMed:25691570}. 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; X07794; CAA30638.1; -; Genomic_DNA. DR EMBL; CP001710; ADL59128.1; -; Genomic_DNA. DR RefSeq; WP_013296338.1; NC_014408.1. DR PDB; 1HBM; X-ray; 1.80 A; C/F=2-249. DR PDB; 1HBN; X-ray; 1.16 A; C/F=2-249. DR PDB; 1HBO; X-ray; 1.78 A; C/F=2-249. DR PDB; 1HBU; X-ray; 1.90 A; C/F=2-249. DR PDB; 1MRO; X-ray; 1.16 A; C/F=2-248. DR PDB; 3M1V; X-ray; 1.45 A; C/F=2-249. DR PDB; 3M2R; X-ray; 1.30 A; C/F=2-249. DR PDB; 3M2U; X-ray; 1.40 A; C/F=2-249. DR PDB; 3M2V; X-ray; 1.80 A; C/F=2-249. DR PDB; 3M30; X-ray; 1.45 A; C/F=2-249. DR PDB; 3M32; X-ray; 1.35 A; C/F=2-249. DR PDB; 3POT; X-ray; 1.20 A; C/F=1-249. DR PDB; 5A0Y; X-ray; 1.10 A; C/F=1-249. DR PDB; 5G0R; X-ray; 1.25 A; C/F=1-249. DR PDB; 7B2H; X-ray; 2.12 A; C/F=1-249. DR PDB; 7SUC; X-ray; 1.90 A; C/c=2-247. DR PDB; 7SXM; X-ray; 2.50 A; C/F=2-247. DR PDBsum; 1HBM; -. DR PDBsum; 1HBN; -. DR PDBsum; 1HBO; -. DR PDBsum; 1HBU; -. DR PDBsum; 1MRO; -. DR PDBsum; 3M1V; -. DR PDBsum; 3M2R; -. DR PDBsum; 3M2U; -. DR PDBsum; 3M2V; -. DR PDBsum; 3M30; -. DR PDBsum; 3M32; -. DR PDBsum; 3POT; -. DR PDBsum; 5A0Y; -. DR PDBsum; 5G0R; -. DR PDBsum; 7B2H; -. DR PDBsum; 7SUC; -. DR PDBsum; 7SXM; -. DR AlphaFoldDB; P11562; -. DR SMR; P11562; -. DR STRING; 79929.MTBMA_c15490; -. DR PaxDb; 79929-MTBMA_c15490; -. DR GeneID; 9705258; -. DR KEGG; mmg:MTBMA_c15490; -. DR PATRIC; fig|79929.8.peg.1502; -. DR HOGENOM; CLU_1092436_0_0_2; -. DR OrthoDB; 52520at2157; -. DR BRENDA; 2.8.4.1; 7427. DR UniPathway; UPA00646; UER00699. DR EvolutionaryTrace; P11562; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IDA:MENGO. 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 /evidence="ECO:0000269|PubMed:2269306" FT CHAIN 2..249 FT /note="Methyl-coenzyme M reductase I subunit gamma" FT /id="PRO_0000147479" FT BINDING 120 FT /ligand="coenzyme M" FT /ligand_id="ChEBI:CHEBI:58319" FT /evidence="ECO:0000269|PubMed:11491299, FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550, FT ECO:0000269|PubMed:27467699, ECO:0007744|PDB:1HBN, FT ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT, FT ECO:0007744|PDB:5A0Y" FT HELIX 10..19 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 33..40 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 65..69 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 74..78 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 82..89 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 98..108 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 127..139 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 156..159 FT /evidence="ECO:0007829|PDB:7B2H" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:5A0Y" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:5A0Y" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 207..213 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:5A0Y" FT HELIX 228..247 FT /evidence="ECO:0007829|PDB:5A0Y" SQ SEQUENCE 249 AA; 28758 MW; E39CD62AD7CCC6DC CRC64; MAQYYPGTTK VAQNRRNFCN PEYELEKLRE ISDEDVVKIL GHRAPGEEYP SVHPPLEEMD EPEDAIREMV EPIDGAKAGD RVRYIQFTDS MYFAPAQPYV RSRAYLCRYR GADAGTLSGR QIIETRERDL EKISKELLET EFFDPARSGV RGKSVHGHSL RLDEDGMMFD MLRRQIYNKD TGRVEMVKNQ IGDELDEPVD LGEPLDEETL MEKTTIYRVD GEAYRDDVEA VEIMQRIHVL RSQGGFNLE //