ID   TALA_SALTY              Reviewed;         316 AA.
AC   Q8ZN83;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Transaldolase A {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=talA {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=STM2473;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00492};
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. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR   EMBL; AE006468; AAL21367.1; -; Genomic_DNA.
DR   RefSeq; NP_461408.1; NC_003197.2.
DR   RefSeq; WP_001072448.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZN83; -.
DR   SMR; Q8ZN83; -.
DR   STRING; 99287.STM2473; -.
DR   PaxDb; Q8ZN83; -.
DR   EnsemblBacteria; AAL21367; AAL21367; STM2473.
DR   GeneID; 1253995; -.
DR   KEGG; stm:STM2473; -.
DR   PATRIC; fig|99287.12.peg.2611; -.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   OMA; DTGDFKQ; -.
DR   PhylomeDB; Q8ZN83; -.
DR   BioCyc; SENT99287:STM2473-MON; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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.
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_0000173612"
FT   ACT_SITE        131
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   316 AA;  35592 MW;  7361CBB6C25A2386 CRC64;
     MNQLDGIKQF TTVVADSGDI ESIRHYQPQD ATTNPSLLLK AAGLEQYGHL IEDAIAWGKK
     HGGTQEQQVA AASDKLAVNF GAEILKSIPG RVSTEVDARL SFDKEKSIEK ARHLVDLYQQ
     QGVDKSRILI KLAATWEGIR AAGQLEKEGI NCNLTLLFSF AQARACAEAG VYLISPFVGR
     IYDWYQARSP LEPYVVEEDP GVKSVRNIYD YFKQHRYETI VMGASFRRTE QILALTGCDR
     LTISPNLLKE LKEKEEPVIR KLVPSSQMFH RPTPMTEAEF RWEHNQDAMA VEKLSEGIRL
     FAVDQRKLED LLAAKL