TAM_ECOSM
ID TAM_ECOSM Reviewed; 252 AA.
AC B1LF96;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=EcSMS35_1653;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000970; ACB17072.1; -; Genomic_DNA.
DR RefSeq; WP_001286571.1; NC_010498.1.
DR AlphaFoldDB; B1LF96; -.
DR SMR; B1LF96; -.
DR EnsemblBacteria; ACB17072; ACB17072; EcSMS35_1653.
DR KEGG; ecm:EcSMS35_1653; -.
DR HOGENOM; CLU_037990_5_2_6; -.
DR OMA; YLAFADH; -.
DR Proteomes; UP000007011; 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_1000129257"
SQ SEQUENCE 252 AA; 28995 MW; 9E1F9A57A4BB559D CRC64;
MSDWNPSLYL HFAAERSRPA VELLARVPLE NIKYVADLGC GPGNSTALLH QRWPAARITG
VDSSPAMIAE ARSALPDCQF VEADIRNWQP EQALDLIFAN ASLQWLPDHY ELFPHLVSLL
NSHGVLAVQM PDNWLEPTHV LMREVAWEQN YPDRGREPLA GVHAYYDILS EAGCEVDIWR
TTYYHQMPSH QAIIDWVTAT GLRPWLQDLT ESEQQHFLTR YHQMLEEQYP LQENGEILLA
FPRLFIVARR TE