ID   MCRZ_METTH              Reviewed;         265 AA.
AC   P21112; O27202; Q50486;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   27-MAR-2024, entry version 142.
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};
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma;
GN   Name=mrtG; OrderedLocusNames=MTH_1130;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=7929010; DOI=10.1128/jb.176.20.6384-6391.1994;
RA   Pihl T.D., Sharma S., Reeve J.N.;
RT   "Growth phase-dependent transcription of the genes that encode the two
RT   methyl coenzyme M reductase isoenzymes and N5-
RT   methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT   Methanobacterium thermoautotrophicum delta H.";
RL   J. Bacteriol. 176:6384-6391(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
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).
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:0000250|UniProtKB:P11562};
CC       Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC       F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is
CC       activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I)
CC       oxidation state. {ECO:0000250|UniProtKB:P11562};
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   -!- 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:0000250|UniProtKB:P11562}.
CC   -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit
CC       family. {ECO:0000305}.
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DR   EMBL; U09990; AAA73438.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB85619.1; -; Genomic_DNA.
DR   PIR; T45149; T45149.
DR   AlphaFoldDB; P21112; -.
DR   SMR; P21112; -.
DR   IntAct; P21112; 1.
DR   STRING; 187420.MTH_1130; -.
DR   PaxDb; 187420-MTH_1130; -.
DR   EnsemblBacteria; AAB85619; AAB85619; MTH_1130.
DR   KEGG; mth:MTH_1130; -.
DR   PATRIC; fig|187420.15.peg.1107; -.
DR   HOGENOM; CLU_1092436_0_0_2; -.
DR   InParanoid; P21112; -.
DR   BioCyc; MetaCyc:MRTGMAUTO-MONOMER; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000005223; 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; 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   Direct protein sequencing; Methanogenesis; Reference proteome; 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_0000147480"
FT   BINDING         123
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P58816"
FT   CONFLICT        132
FT                   /note="D -> V (in Ref. 1; AAA73438)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="D -> DD (in Ref. 1; AAA73438)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  30567 MW;  F1E6783AAE7A3CA8 CRC64;
     MTYKAQYTPG ETQIAENRRK HMDPDYEFRK LREVSDEDLV KVLGHRNPGE SYKSVHPPLD
     EMDFEEDIVR DMVEPIQGAK EGVRVRYIQF ADSMYNAPAQ PYDRARTYMW RYRGVDTGTL
     SGRQVIEMRE LDLEGVSKEL VETELFDPAT TGIRGATVHG HSLRLDENGL MFDALQRYVF
     DEEKGHVVYV KDQVGRPLDE PVDMGQPLGE DELKKITTIY RKDNIAMRDD KEAIEVVENI
     HTGRTMGGFG MDVFKDDLRK RLGDD
//