ID   TAM_METS4               Reviewed;         257 AA.
AC   B0UPF4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=M446_5272;
OS   Methylobacterium sp. (strain 4-46).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4-46;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000943; ACA19596.1; -; Genomic_DNA.
DR   RefSeq; WP_012334981.1; NC_010511.1.
DR   AlphaFoldDB; B0UPF4; -.
DR   SMR; B0UPF4; -.
DR   STRING; 426117.M446_5272; -.
DR   EnsemblBacteria; ACA19596; ACA19596; M446_5272.
DR   KEGG; met:M446_5272; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_037990_5_2_5; -.
DR   OMA; RFDARYY; -.
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..257
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_1000129261"
SQ   SEQUENCE   257 AA;  28029 MW;  8271EF59B0BCD9D9 CRC64;
     MADWNAAQYL KFADERTRPA ADLLARVPLE SPARVIDLGC GPGNSTALLC ARFPRAAVTG
     LDSSPDMLAT ARERLPAVRF VEADLAGFTP AEPPDLLFAN AVLQWLPDHA GLLARLARML
     APGGCLAVQM PDNLEEPSHR LMRRVAGEAP FAERLAQAAA ARTRLGSFRD YDAWLSAAGC
     TVDLWRTTYV HPLAGHRGIV EWVRGTGLRP FLDPLDPADQ AAFLARYEAA LAEAYPPQAD
     GRVLLPFPRL FLVARRR