TAM_ECOSE
ID TAM_ECOSE Reviewed; 252 AA.
AC B6IAS2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=ECSE_1609;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
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; AP009240; BAG77133.1; -; Genomic_DNA.
DR RefSeq; WP_001286567.1; NC_011415.1.
DR AlphaFoldDB; B6IAS2; -.
DR SMR; B6IAS2; -.
DR EnsemblBacteria; BAG77133; BAG77133; ECSE_1609.
DR KEGG; ecy:ECSE_1609; -.
DR HOGENOM; CLU_037990_5_2_6; -.
DR OMA; YLAFADH; -.
DR Proteomes; UP000008199; 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; 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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..252
FT /note="Trans-aconitate 2-methyltransferase"
FT /id="PRO_1000129256"
SQ SEQUENCE 252 AA; 29057 MW; 7B9BCB16B1572DD7 CRC64;
MSDWNPSLYL HFAAERSRPA VELLARVPLE NIKYVADLGC GPGNSTALLH QRWPAARITG
IDSSPAMIAE ARSALPDCQF VEADIRNWQP EQALDLIFAN ASLQWLPDHY ELFPHLVSLL
NPQGVLAVQM PDNWLEPTHV LMREVAWEQN YPDRGREPLA GVHAYYDILS EAGCEVDIWR
TTYYHQMPSH QAIIDWVTAT GLRPWLQDLT ESEQQLFLTR YHQMLEEQYP LQENEQILLA
FPRLFIVARR TE