ID   TAL_CAMJR               Reviewed;         325 AA.
AC   Q5HWI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   10-JUN-2026, entry version 96.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00493}; OrderedLocusNames=CJE0329;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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_00493}.
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_00493};
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_00493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00493}.
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DR   EMBL; CP000025; AAW34919.1; -; Genomic_DNA.
DR   RefSeq; WP_002851728.1; NC_003912.7.
DR   AlphaFoldDB; Q5HWI6; -.
DR   SMR; Q5HWI6; -.
DR   KEGG; cjr:CJE0329; -.
DR   HOGENOM; CLU_050771_1_0_7; -.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00955; Transaldolase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00493; Transaldolase_2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004732; Transaldolase_2.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   NCBIfam; NF003026; PRK03903.1; 1.
DR   NCBIfam; TIGR00876; tal_mycobact; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PIRSF; PIRSF036915; Trnald_Bac_Plnt; 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..325
FT                   /note="Transaldolase"
FT                   /id="PRO_1000026522"
FT   ACT_SITE        94
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   ACT_SITE        125
FT                   /note="Nucleophile; Schiff-base intermediate with
FT                   substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   BINDING         9
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   BINDING         34
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   BINDING         125
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   BINDING         147
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   BINDING         191
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
FT   BINDING         196
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   325 AA;  36917 MW;  B6AAB6654E877E45 CRC64;
     MKNFSLWCDF IENSFLDNEF LNLLSHGING ATSNPAIFKN AILNSPIYKD KILKLKEKKT
     KDIYEELAIS DIQKAADKLA PLFYQKNDGF ISIEIDPRLH DNTTLSLGEA KRLYSAIGKE
     NIMIKIPATK ASYEVMYELM KNGISVNATL IFSLEQSQKC FEALNAGLVE FRKNNIALKE
     QNTRTPQAVI SIFVSRFDRL LNPKAKEQNR IGILNANLAY NNIYSKNEPN IRALFASTGV
     KGDDLPKDYY IKELLFENSV NTAPLDAIEA FKGKMHFKKP LMNFEIYTEL NQIISQSERE
     KACNDLLSDG LEQFCIAFED ILKAL
//