ID   MTAA_METBA              Reviewed;         339 AA.
AC   Q48927;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Methylcobamide:CoM methyltransferase MtaA;
DE            EC=2.1.1.246;
DE   AltName: Full=Methylcobalamin: Coenzyme M methyltransferase;
DE   AltName: Full=Methylcobamide:CoM methyltransferase II isozyme M;
DE            Short=MT2-M;
DE   AltName: Full=[Methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase;
GN   Name=mtaA; Synonyms=cmtM;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-21 AND 88-94,
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=NIH;
RX   PubMed=8702528; DOI=10.1074/jbc.271.31.18725;
RA   Leclerc G.M., Grahame D.A.;
RT   "Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina
RT   barkeri: physicochemical characterization, cloning, sequence analysis, and
RT   heterologous gene expression.";
RL   J. Biol. Chem. 271:18725-18731(1996).
CC   -!- FUNCTION: Methyltransferase involved in methanogenesis in the methanol
CC       pathway. Catalyzes the transfer of the methyl group from the methylated
CC       corrinoid protein MtaC to coenzyme M, forming the substrate for
CC       coenzyme-B sulfoethylthiotransferase. MtaC can be substituted by free
CC       cob(I)alamin in vitro. {ECO:0000269|PubMed:8702528}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme M + methyl-Co(III)-[methanol-specific corrinoid
CC         protein] = Co(I)-[methanol-specific corrinoid protein] + H(+) +
CC         methyl-coenzyme M; Xref=Rhea:RHEA:45208, Rhea:RHEA-COMP:17570,
CC         Rhea:RHEA-COMP:17571, ChEBI:CHEBI:15378, ChEBI:CHEBI:16379,
CC         ChEBI:CHEBI:58286, ChEBI:CHEBI:58319, ChEBI:CHEBI:60494;
CC         EC=2.1.1.246; Evidence={ECO:0000269|PubMed:8702528};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:8702528};
CC       Note=Zn(2+) is involved in coenzyme M activation: in the absence of
CC       coenzyme M, zinc is coordinated by a single sulfur ligand and three
CC       oxygen or nitrogen ligands. In the presence of coenzyme M, one
CC       oxygen/nitrogen-ligand is replaced by sulfur, probably due to ligation
CC       of the thiol group of coenzyme M. {ECO:0000269|PubMed:8702528};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10 mM for 3-mercaptopropionate {ECO:0000269|PubMed:8702528};
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       MtbA/mtaA subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U38918; AAC44213.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48927; -.
DR   SMR; Q48927; -.
DR   SABIO-RK; Q48927; -.
DR   GO; GO:1990088; F:[methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   CDD; cd03307; Mta_CmuA_like; 1.
DR   Gene3D; 3.20.20.210; -; 1.
DR   InterPro; IPR006360; Mtase_MtaA_CmuA.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; SSF51726; 1.
DR   TIGRFAMs; TIGR01463; mtaA_cmuA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Methanogenesis;
KW   Methyltransferase; Transferase; Zinc.
FT   CHAIN           1..339
FT                   /note="Methylcobamide:CoM methyltransferase MtaA"
FT                   /id="PRO_0000418940"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   339 AA;  35933 MW;  081A43DD3DD9E41E CRC64;
     MSEFTLKTRL LAALEGKPVD KVPVCSVTQT GIVELMDEVG AAWPEAHTNP ELMAKLAIAN
     YELSGLEAVR LPYCLTVLGE AMGCEINMGT KNRQPSVTAS PYPKNLDGAA VPADLLQRNR
     IPAVLEAIKI VREKVGPDVP IIGGMEGPVT LASDLISVKS FMKWSIKKTD LFEQALDIST
     EAAIAYANAM VEAGADVIAI ADPVASPDLM SPDTFRQFLQ SRLQKFSASV NSVTVLHICG
     KVNAILSDMA DCGFEGLSVE EKIGDAAEGK KVIGDRARLV GNISSPFTLL PGPIDKIKAE
     AKVALEGGID VLAPGCGIAP MTPLENIKAL VAARDEYYA