MCRG_METBF
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 03-AUG-2022, entry version 145.
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}.
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DR EMBL; Y00158; CAA68356.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ69868.1; -; Genomic_DNA.
DR PIR; D29525; D29525.
DR RefSeq; WP_011305917.1; NC_007355.1.
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 PRIDE; P07964; -.
DR EnsemblBacteria; AAZ69868; AAZ69868; Mbar_A0894.
DR GeneID; 3625939; -.
DR KEGG; mba:Mbar_A0894; -.
DR eggNOG; arCOG04858; Archaea.
DR HOGENOM; CLU_1092436_0_0_2; -.
DR OMA; GHRNPGE; -.
DR OrthoDB; 51032at2157; -.
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; -; 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 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
