ID   TAM_MYCTO               Reviewed;         261 AA.
AC   P9WGA2; L0T4Y3; O53698; P66885;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Probable trans-aconitate 2-methyltransferase;
DE            EC=2.1.1.144 {ECO:0000255|HAMAP-Rule:MF_00560};
GN   Name=tam {ECO:0000255|HAMAP-Rule:MF_00560}; OrderedLocusNames=MT0307;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44531.1; -; Genomic_DNA.
DR   PIR; D70837; D70837.
DR   RefSeq; WP_003401538.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGA2; -.
DR   SMR; P9WGA2; -.
DR   EnsemblBacteria; AAK44531; AAK44531; MT0307.
DR   GeneID; 45424268; -.
DR   KEGG; mtc:MT0307; -.
DR   PATRIC; fig|83331.31.peg.330; -.
DR   HOGENOM; CLU_037990_5_2_11; -.
DR   Proteomes; UP000001020; 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; 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..261
FT                   /note="Probable trans-aconitate 2-methyltransferase"
FT                   /id="PRO_0000428397"
SQ   SEQUENCE   261 AA;  29268 MW;  B92D46F1A5BA7A02 CRC64;
     MWDPDVYLAF SGHRNRPFYE LVSRVGLERA RRVVDLGCGP GHLTRYLARR WPGAVIEALD
     SSPEMVAAAA ERGIDATTGD LRDWKPKPDT DVVVSNAALH WVPEHSDLLV RWVDELAPGS
     WIAVQIPGNF ETPSHAAVRA LARREPYAKL MRDIPFRVGA VVQSPAYYAE LLMDTGCKVD
     VWETTYLHQL TGEHPVLDWI TGSALVPVRE RLSDESWQQF RQELIPLLND AYPPRADGST
     IFPFRRLFMV AEVGGARRSG G