ID   MTBA_METAC              Reviewed;         339 AA.
AC   P58869;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Methylcobamide:CoM methyltransferase MtbA;
DE            EC=2.1.1.247;
DE   AltName: Full=MT2-A;
DE   AltName: Full=Methylcobamide:CoM methyltransferase II isozyme A;
DE   AltName: Full=[Methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M;
GN   Name=mtbA; OrderedLocusNames=MA_0146;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- FUNCTION: Methyltransferase involved in methanogenesis from
CC       methylamines methanol pathway. Catalyzes the transfer of the methyl
CC       group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) to
CC       coenzyme M, forming the substrate for coenzyme-B
CC       sulfoethylthiotransferase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme M + methyl-Co(III)-[methylamine-specific corrinoid
CC         protein] = Co(I)-[methylamine-specific corrinoid protein] + H(+) +
CC         methyl-coenzyme M; Xref=Rhea:RHEA:18773, Rhea:RHEA-COMP:11120,
CC         Rhea:RHEA-COMP:11121, ChEBI:CHEBI:15378, ChEBI:CHEBI:58286,
CC         ChEBI:CHEBI:58319, ChEBI:CHEBI:85033, ChEBI:CHEBI:85035;
CC         EC=2.1.1.247;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from methylated amine.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       MtbA/MtaA subfamily. {ECO:0000305}.
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DR   EMBL; AE010299; AAM03599.1; -; Genomic_DNA.
DR   RefSeq; WP_011020204.1; NC_003552.1.
DR   AlphaFoldDB; P58869; -.
DR   SMR; P58869; -.
DR   STRING; 188937.MA_0146; -.
DR   EnsemblBacteria; AAM03599; AAM03599; MA_0146.
DR   GeneID; 1472038; -.
DR   KEGG; mac:MA_0146; -.
DR   HOGENOM; CLU_040933_2_1_2; -.
DR   InParanoid; P58869; -.
DR   OMA; GAYWPEA; -.
DR   OrthoDB; 21172at2157; -.
DR   PhylomeDB; P58869; -.
DR   UniPathway; UPA00650; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0043833; F:[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase activity; 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   3: Inferred from homology;
KW   Metal-binding; Methanogenesis; Methyltransferase; Reference proteome;
KW   Transferase; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..339
FT                   /note="Methylcobamide:CoM methyltransferase MtbA"
FT                   /id="PRO_0000187668"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
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;  36821 MW;  36F8CE0437FAF0A7 CRC64;
     MTEYTPKERL YRALRKQPVD RMPAVCFTQT ATVEQMEASG AYWPEAHADA EKMATLAEAG
     HTVIGFEAVR VPFDITAEAE LFGCGIKAGD LKQQPSVIKH VVKNMEDMEK LKGYSLNEGR
     VGLILEAIKI LSEKYGKELP IIGSMIGPFS LAQHINGDAW FGNLFTGEEI VPALLDFCSD
     FNVAYAKAMV ENGADTIAII DPTASYELIG GEFYEKYALP YQKKIVDAMK ELDVGTVLHI
     CGNTTNGLSI MDKTGVNGIS VDQRVDIKTA TDNVENAIII GNLDPVAILW NGTPEDVAEA
     SKKVLDVGVG LLSPGCGIVS MTPSANLQKM VECAKNYKY