ID   TAM_VARPS               Reviewed;         259 AA.
AC   C5CSI6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=Vapar_1433;
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S110;
RX   PubMed=21183664; DOI=10.1128/jb.00925-10;
RA   Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA   O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA   Ovchinnikova G., Goodwin L., Han C.;
RT   "Complete genome sequence of the metabolically versatile plant growth-
RT   promoting endophyte, Variovorax paradoxus S110.";
RL   J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS18084.1; -; Genomic_DNA.
DR   RefSeq; WP_012746578.1; NC_012791.1.
DR   AlphaFoldDB; C5CSI6; -.
DR   SMR; C5CSI6; -.
DR   STRING; 543728.Vapar_1433; -.
DR   PRIDE; C5CSI6; -.
DR   EnsemblBacteria; ACS18084; ACS18084; Vapar_1433.
DR   GeneID; 45055739; -.
DR   KEGG; vap:Vapar_1433; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_037990_5_2_4; -.
DR   OMA; YLAFADH; -.
DR   OrthoDB; 1739932at2; -.
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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR   InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..259
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_1000212043"
SQ   SEQUENCE   259 AA;  28895 MW;  8EBEFA575AB5DCD6 CRC64;
     MLDWNPALYR RYEDERTRPA QELLARVPLP EAARVVDLGC GPGNSTELLA NRFPTAKVVG
     TDNSEAMLAS ARERLPQARF ELSDIATWAP QDQAPDLIYA NAALQWVPDH EQLIPRLFAA
     LAPGGVLAIQ MPDNREEPTH RLMRAVAAEA PWAEPIGNAD RLRTLLLPLG GYYDLLAPAA
     ARVDVWHTIY QHPMADAAAI VEWVRGTGLK PFVDRLPADL QASYLAEYER RVDQAYPVRT
     DGKRLLAFPR MFIVAQKKA