ID   TAL2_SALPA              Reviewed;         316 AA.
AC   Q5PCU4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   10-JUN-2026, entry version 101.
DE   RecName: Full=Transaldolase 2 {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=tal2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   OrderedLocusNames=SPA0396;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Transaldolase involved in the non-oxidative phase in the
CC       pentose phosphate pathway. Catalyzes the reversible conversion of
CC       sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC       erythrose-4-phosphate and beta-D-fructose 6-phosphate. Transaldolase is
CC       important for the balance of metabolites in the pentose-phosphate
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate =
CC         D-erythrose 4-phosphate + beta-D-fructose 6-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:0000255|HAMAP-Rule:MF_00492}.
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; CP000026; AAV76407.1; -; Genomic_DNA.
DR   RefSeq; WP_001072450.1; NC_006511.1.
DR   AlphaFoldDB; Q5PCU4; -.
DR   SMR; Q5PCU4; -.
DR   KEGG; spt:SPA0396; -.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 3.20.20.70:FF:000002; Transaldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; NF009001; PRK12346.1; 1.
DR   NCBIfam; TIGR00874; talAB; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF16; TRANSALDOLASE A; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT   CHAIN           1..316
FT                   /note="Transaldolase 2"
FT                   /id="PRO_0000230970"
FT   ACT_SITE        95
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   ACT_SITE        131
FT                   /note="Nucleophile; Schiff-base intermediate with
FT                   substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         16
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         34
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         131
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         153
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         175
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         180
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         225
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         227
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   316 AA;  35538 MW;  D7F9B77FDAFD5D15 CRC64;
     MNQLDGIKQF TTVVADSGDI ESIRHYQPQD ATTNPSLLLK AAGLEQYGHL IEDAIAWGKK
     HGGTQEQQVA AASDKLAVNF GAEILKSIPG RVSTEVDARL SFDKEKSIEK ARHLVGLYQQ
     QGIDKSRILI KLAATWEGIR AAGQLEKEGI NCNLTLLFSF AQARACAEAG VYLISPFVGR
     IYDWYQARSP LEPYVVEEDP GVKSVRNIYD YFKQHRYETI VMGASFRRTE QILALTGCDR
     LTISPNLLKE LKEKEEPVIR KLVPSSQMFH RPTSMTEAEF RWEHNQDAMA VEKLSEGIRL
     FAVDQRKLED LLAAKL
//