MCRZ_METTH
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 03-AUG-2022, entry version 136.
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 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 OMA; GHRNPGE; -.
DR BioCyc; MetaCyc:MRTGMAUTO-MON; -.
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; -; 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 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
