TAM_ECO57
ID TAM_ECO57 Reviewed; 252 AA.
AC Q8XAZ2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Trans-aconitate 2-methyltransferase;
DE EC=2.1.1.144;
GN Name=tam; OrderedLocusNames=Z2186, ECs2126;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification
CC of trans-aconitate at high affinity and of cis-aconitate, isocitrate,
CC and citrate at lower velocities and affinities. {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Tam family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG56247.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35549.1; -; Genomic_DNA.
DR PIR; C85723; C85723.
DR PIR; F90894; F90894.
DR RefSeq; NP_310153.1; NC_002695.1.
DR RefSeq; WP_001286577.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XAZ2; -.
DR SMR; Q8XAZ2; -.
DR STRING; 155864.EDL933_2119; -.
DR EnsemblBacteria; AAG56247; AAG56247; Z2186.
DR EnsemblBacteria; BAB35549; BAB35549; ECs_2126.
DR GeneID; 917326; -.
DR KEGG; ece:Z2186; -.
DR KEGG; ecs:ECs_2126; -.
DR PATRIC; fig|386585.9.peg.2232; -.
DR eggNOG; COG4106; Bacteria.
DR HOGENOM; CLU_037990_5_2_6; -.
DR OMA; YLAFADH; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..252
FT /note="Trans-aconitate 2-methyltransferase"
FT /id="PRO_0000218081"
SQ SEQUENCE 252 AA; 28947 MW; BEEE2470E3E209A1 CRC64;
MSDWNPSLYL HFAAERSRPA VELLARVPLE NVDYVADLGC GPGNSTALLH QRWPAARITG
IDSSPAMIAE ARSALPDCQF VEADIRNWQP EQALDLIFAN ASLQWLPDHY ELFPHLVSLL
NPQGVLAVQM PDNWLEPTHV LMREVAWEQN YPDRGRESLA GVHAYYDILS EAGCEVDIWR
TTYYHQMPSH QAIIDWVTAT GLRPWLQDLT ESEQQLFLTR YHQMLKEQYP LQENGQILLA
FPRLFIVARR TE