ID   TAL_CAMJE               Reviewed;         325 AA.
AC   Q9PIL5; Q0PBM5;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=Cj0281c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL111168; CAL34434.1; -; Genomic_DNA.
DR   PIR; G81446; G81446.
DR   RefSeq; WP_002851728.1; NC_002163.1.
DR   RefSeq; YP_002343722.1; NC_002163.1.
DR   AlphaFoldDB; Q9PIL5; -.
DR   SMR; Q9PIL5; -.
DR   IntAct; Q9PIL5; 9.
DR   STRING; 192222.Cj0281c; -.
DR   PaxDb; Q9PIL5; -.
DR   PRIDE; Q9PIL5; -.
DR   EnsemblBacteria; CAL34434; CAL34434; Cj0281c.
DR   GeneID; 904605; -.
DR   KEGG; cje:Cj0281c; -.
DR   PATRIC; fig|192222.6.peg.274; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_7; -.
DR   OMA; ATECYYQ; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000799; Chromosome.
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; -; 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   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR   TIGRFAMs; TIGR00876; tal_mycobact; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..325
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173630"
FT   ACT_SITE        125
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
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