ID   TAL_ACTP2               Reviewed;         315 AA.
AC   A3MYD4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   10-JUN-2026, entry version 114.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00492};
GN   OrderedLocusNames=APL_0062;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73170.1; -; Genomic_DNA.
DR   RefSeq; WP_011848304.1; NC_009053.1.
DR   AlphaFoldDB; A3MYD4; -.
DR   SMR; A3MYD4; -.
DR   STRING; 416269.APL_0062; -.
DR   EnsemblBacteria; ABN73170; ABN73170; APL_0062.
DR   KEGG; apl:APL_0062; -.
DR   PATRIC; fig|416269.6.peg.64; -.
DR   eggNOG; COG0176; Bacteria.
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:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT   CHAIN           1..315
FT                   /note="Transaldolase"
FT                   /id="PRO_1000014482"
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         224
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         226
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   315 AA;  34794 MW;  ECD56E5E0046E67B CRC64;
     MSQLDALREM TVVVADTGDI EAIKQYQPQD ATTNPSLILS ASALPQYASL IDDAVAYAKA
     RSDDKAQLLI DAEDKLAVNI GLEILKIVPG RISTEVDARL SYDTKATIEK ARQIMKLYND
     AGISNDRILI KIASTWQGIR AAEVLEKEGI NCNLTLLFSQ AQARACAKAG VYLISPFVGR
     ILDWYKAAEK KEYAPAEDPG VISVTNIYNY YKQYGYQTVV MGASFRNVGE ITEIAGCDRL
     TIAPPLLKEL AESNAPLVRK LEYKGEVKTR PAPLTEAEFY WQHNQDPMAV EKLAEGIRKF
     AVDIEKLEAM LAAKL
//