MCRG_METTM
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 03-AUG-2022, entry version 137.
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}.
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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 EnsemblBacteria; ADL59128; ADL59128; 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 OMA; IMGHRQP; -.
DR OrthoDB; 51032at2157; -.
DR BRENDA; 2.8.4.1; 25952.
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; -; 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 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
