ID   TAM_BRUA4               Reviewed;         255 AA.
AC   A6WZN1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Oant_1719;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(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; CP000758; ABS14435.1; -; Genomic_DNA.
DR   RefSeq; WP_012091728.1; NC_009667.1.
DR   AlphaFoldDB; A6WZN1; -.
DR   SMR; A6WZN1; -.
DR   STRING; 439375.Oant_1719; -.
DR   EnsemblBacteria; ABS14435; ABS14435; Oant_1719.
DR   KEGG; oan:Oant_1719; -.
DR   PATRIC; fig|439375.7.peg.1816; -.
DR   eggNOG; COG4106; Bacteria.
DR   HOGENOM; CLU_037990_5_2_5; -.
DR   OMA; RFDARYY; -.
DR   OrthoDB; 1739932at2; -.
DR   PhylomeDB; A6WZN1; -.
DR   Proteomes; UP000002301; Chromosome 1.
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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023506; Trans-aconitate_MeTrfase.
DR   InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..255
FT                   /note="Trans-aconitate 2-methyltransferase"
FT                   /id="PRO_1000056570"
SQ   SEQUENCE   255 AA;  28662 MW;  BBC95B977FD8C1F6 CRC64;
     MKDWSAKQYL KFEDERSRPA RDLLAQIPVD KPRKVVDIGC GPGNSTELLV ERWPEADVSG
     FDTSPDMIEK AKVRLPKVDF TIGDVASYEP DAETDVLFSN AVFQWLPDHI KQMKRLLSLL
     RPGAVLAVQM PDNMGEQTHV GMRDVAKTEA FAAKIGAKGR GPLPPVMEYY NALAGQAARL
     DIWHTVYNHP LDGVDAIVEW VKATGLRPFL DPLDEQEQAD YLKAYKARIA PHYPVAVDGK
     VLLRFPRIFL VVQKR