ID   TAM_ECO55               Reviewed;         252 AA.
AC   B7L7L9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Trans-aconitate 2-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00560};
DE            EC=2.1.1.144 {ECO:0000255|HAMAP-Rule:MF_00560};
GN   Name=tam {ECO:0000255|HAMAP-Rule:MF_00560}; OrderedLocusNames=EC55989_1652;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC       of trans-aconitate. {ECO:0000255|HAMAP-Rule:MF_00560}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00560};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00560}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC       {ECO:0000255|HAMAP-Rule:MF_00560}.
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DR   EMBL; CU928145; CAU97505.1; -; Genomic_DNA.
DR   RefSeq; WP_001286556.1; NC_011748.1.
DR   AlphaFoldDB; B7L7L9; -.
DR   SMR; B7L7L9; -.
DR   EnsemblBacteria; CAU97505; CAU97505; EC55989_1652.
DR   KEGG; eck:EC55989_1652; -.
DR   HOGENOM; CLU_037990_5_2_6; -.
DR   OMA; YLAFADH; -.
DR   Proteomes; UP000000746; Chromosome.
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; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR   InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..252
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_1000196654"
SQ   SEQUENCE   252 AA;  28937 MW;  8899F12D2B84BD58 CRC64;
     MSDWNPSLYL HFAAERSRPA VELLARVPLE NIEYVADLGC GPGNSTALLN QRWPAARITG
     IDSSPAMIAE ARSALPDCQF VEADIRNWQP EQALDLIFAN ASLQWLPDHY ELFPHLVSLL
     NPQGVLAVQM PDNWLEPTHV LMREVAWEQN YPDRGRESLA GIHAYYDILS EAGCEVDIWR
     TTYYHQMPSH QAIIDWVTAT GLRPWLQDLA ESEQQLFLTR YHQMLEEQYP LQENGQILLA
     FPRLFIVARR TE