ID   TAM_ECOLI               Reviewed;         252 AA.
AC   P76145; Q2MB97;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Trans-aconitate 2-methyltransferase;
DE            EC=2.1.1.144 {ECO:0000269|PubMed:10224113};
GN   Name=tam; Synonyms=yneD; OrderedLocusNames=b1519, JW1512;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10224113; DOI=10.1074/jbc.274.19.13470;
RA   Cai H., Clarke S.;
RT   "A novel methyltransferase catalyzes the methyl esterification of trans-
RT   aconitate in Escherichia coli.";
RL   J. Biol. Chem. 274:13470-13479(1999).
CC   -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC       of trans-aconitate at high affinity and of cis-aconitate, isocitrate,
CC       and citrate at lower velocities and affinities.
CC       {ECO:0000269|PubMed:10224113}.
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:0000269|PubMed:10224113};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14970;
CC         Evidence={ECO:0000305|PubMed:10224113};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.2 mM for trans-aconitate {ECO:0000269|PubMed:10224113};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10224113}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74592.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76459.1; -; Genomic_DNA.
DR   PIR; B64906; B64906.
DR   RefSeq; NP_416036.1; NC_000913.3.
DR   RefSeq; WP_001286597.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P76145; -.
DR   SMR; P76145; -.
DR   BioGRID; 4260219; 21.
DR   IntAct; P76145; 1.
DR   STRING; 511145.b1519; -.
DR   jPOST; P76145; -.
DR   PaxDb; P76145; -.
DR   PRIDE; P76145; -.
DR   EnsemblBacteria; AAC74592; AAC74592; b1519.
DR   EnsemblBacteria; BAE76459; BAE76459; BAE76459.
DR   GeneID; 946074; -.
DR   KEGG; ecj:JW1512; -.
DR   KEGG; eco:b1519; -.
DR   PATRIC; fig|1411691.4.peg.748; -.
DR   EchoBASE; EB3573; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_037990_5_2_6; -.
DR   InParanoid; P76145; -.
DR   OMA; YLAFADH; -.
DR   PhylomeDB; P76145; -.
DR   BioCyc; EcoCyc:G6806-MON; -.
DR   BioCyc; MetaCyc:G6806-MON; -.
DR   SABIO-RK; P76145; -.
DR   PRO; PR:P76145; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0030798; F:trans-aconitate 2-methyltransferase activity; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..252
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_0000218080"
SQ   SEQUENCE   252 AA;  29006 MW;  917BB2F7F1858B4A CRC64;
     MSDWNPSLYL HFSAERSRPA VELLARVPLE NVEYVADLGC GPGNSTALLQ QRWPAARITG
     IDSSPAMIAE ARSALPDCQF VEADIRNWQP VQALDLIFAN ASLQWLPDHY ELFPHLVSLL
     NPQGVLAVQM PDNWLEPTHV LMREVAWEQN YPDRGREPLA GVHAYYDILS EAGCEVDIWR
     TTYYHQMPSH QAIIDWVTAT GLRPWLQDLT ESEQQLFLKR YHQMLEEQYP LQENGQILLA
     FPRLFIVARR ME