ID   TAM_BRUME               Reviewed;         255 AA.
AC   Q8YI91;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Trans-aconitate 2-methyltransferase;
DE            EC=2.1.1.144;
GN   Name=tam; OrderedLocusNames=BMEI0554;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC       of trans-aconitate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + trans-aconitate = (E)-3-
CC         (methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:14969, ChEBI:CHEBI:15708, ChEBI:CHEBI:57470,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.144;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL51735.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL51735.1; ALT_FRAME; Genomic_DNA.
DR   PIR; AD3321; AD3321.
DR   STRING; 224914.BMEI0554; -.
DR   EnsemblBacteria; AAL51735; AAL51735; BMEI0554.
DR   KEGG; bme:BMEI0554; -.
DR   eggNOG; COG4106; Bacteria.
DR   Proteomes; UP000000419; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030798; F:trans-aconitate 2-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.290; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00560; Tran_acon_Me_trans; 1.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR   InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..255
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_0000218077"
SQ   SEQUENCE   255 AA;  28568 MW;  B1AA641CEEBADAC5 CRC64;
     MKDWSAKQYL KFEDEXSRPA RDLLAQIPLS APRKVVDIGC GPGNSTKLLV ERWPDAQISG
     FDTSPDMIDT AKTHLPDVEF FISDAASFEP DAETDVLFSN AVFQWLPDHV EQLQRLLSLL
     QPGAFLAVQM PDNMGEQTHV GMRDVAKTAP FAMEIATKGR AALPPVATYY NAFADDAARI
     DIWHTIYNHP LAGVDAIVEW VKGTGLRPFL DPLDEQEQAD YLKAYKARIA EHYPMTADGK
     VLLRFPRIFL VVQKK