ID   TALA_ECO57              Reviewed;         316 AA.
AC   P0A869; P78258; P80218;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Transaldolase A;
DE            EC=2.2.1.2;
GN   Name=talA; OrderedLocusNames=Z3720, ECs3326;
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: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC       step 2/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG57573.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36749.1; -; Genomic_DNA.
DR   PIR; A85889; A85889.
DR   PIR; F91044; F91044.
DR   RefSeq; NP_311353.1; NC_002695.1.
DR   RefSeq; WP_001003709.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A869; -.
DR   SMR; P0A869; -.
DR   STRING; 155864.EDL933_3618; -.
DR   EnsemblBacteria; AAG57573; AAG57573; Z3720.
DR   EnsemblBacteria; BAB36749; BAB36749; ECs_3326.
DR   GeneID; 66673675; -.
DR   GeneID; 915272; -.
DR   KEGG; ece:Z3720; -.
DR   KEGG; ecs:ECs_3326; -.
DR   PATRIC; fig|386585.9.peg.3473; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   OMA; DTGDFKQ; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..316
FT                   /note="Transaldolase A"
FT                   /id="PRO_0000173591"
FT   ACT_SITE        131
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  35659 MW;  990B00ED7937CF19 CRC64;
     MNELDGIKQF TTVVADSGDI ESIRHYHPQD ATTNPSLLLK AAGLSQYEHL IDDAIAWGKK
     NGKTQEQQVV AACDKLAVNF GAEILKIVPG RVSTEVDARL SFDKEKSIEK ARHLVDLYQQ
     QGVEKSRILI KLASTWEGIR AAEELEKEGI NCNLTLLFSF AQARACAEAG VFLISPFVGR
     IYDWYQARKP MDPYVVEEDP GVKSVRNIYD YYKQHHYETI VMGASFRRTE QILALTGCDR
     LTIAPNLLKE LQEKVSPVVR KLIPPSQTFP RPAPMSEAEF RWEHNQDAMA VEKLSEGIRL
     FAVDQRKLED LLAAKL