MCRZ_METTM
ID MCRZ_METTM Reviewed; 265 AA.
AC P58816; D9PXZ4;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Methyl-coenzyme M reductase II subunit gamma {ECO:0000303|PubMed:2269306};
DE Short=MCR II gamma {ECO:0000303|PubMed:2269306};
DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306};
GN Name=mrtG; OrderedLocusNames=MTBMA_c15130;
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 [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 [2]
RP PROTEIN SEQUENCE OF 2-15, 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 [3] {ECO:0007744|PDB:5A8R}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP 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=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).
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:0000269|PubMed:2269306}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000305|PubMed:2269306};
CC -!- COFACTOR:
CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC Evidence={ECO:0000269|PubMed:27467699};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid. {ECO:0000269|PubMed:27467699};
CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC from methyl-coenzyme M: step 1/1. {ECO:0000305|PubMed:2269306}.
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:27467699}.
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 -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit
CC family. {ECO:0000305}.
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DR EMBL; CP001710; ADL59092.1; -; Genomic_DNA.
DR PIR; E69017; E69017.
DR RefSeq; WP_013296303.1; NC_014408.1.
DR PDB; 5A8R; X-ray; 2.15 A; C/F/I/L=1-265.
DR PDBsum; 5A8R; -.
DR AlphaFoldDB; P58816; -.
DR SMR; P58816; -.
DR STRING; 79929.MTBMA_c15130; -.
DR EnsemblBacteria; ADL59092; ADL59092; MTBMA_c15130.
DR GeneID; 9705222; -.
DR KEGG; mmg:MTBMA_c15130; -.
DR PATRIC; fig|79929.8.peg.1466; -.
DR HOGENOM; CLU_1092436_0_0_2; -.
DR OMA; GHRNPGE; -.
DR OrthoDB; 51032at2157; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000000345; Chromosome.
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; Direct protein sequencing; Methanogenesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2269306"
FT CHAIN 2..265
FT /note="Methyl-coenzyme M reductase II subunit gamma"
FT /id="PRO_0000147481"
FT BINDING 123
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:27467699,
FT ECO:0007744|PDB:5A8R"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5A8R"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 231..249
FT /evidence="ECO:0007829|PDB:5A8R"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:5A8R"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:5A8R"
SQ SEQUENCE 265 AA; 30535 MW; EA917838AE5A3CA9 CRC64;
MSYKAQYTPG ETQIAENRRK HMDPDYEFRK LREVSDEDLV KVLGHRNPGE SYKSVHPPLD
EMDFEEDIVR DMVEPIQGAK EGVRVRYIQF ADSMYNAPAQ PYDRARTYMW RYRGVDTGTL
SGRQVIEMRE LDLEGVSKEL VETELFDPAT TGIRGATVHG HSLRLDENGL MFDALQRYVF
DEEKGHVVYV KDQVGRPLDE PVDMGQPLGE DELKKITTIY RKDNIAMRDD KEAIEVVENI
HTGRTLGGFG MDVFKDDLRK RLGDD
