ID   TAL1_KLULA              Reviewed;         334 AA.
AC   P34214;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=TAL1; OrderedLocusNames=KLLA0A02607g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=7934848; DOI=10.1111/j.1365-2958.1993.tb00957.x;
RA   Jacoby J., Hollenberg C.P., Heinisch J.J.;
RT   "Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence
RT   that glucose can be metabolized through the pentose phosphate pathway.";
RL   Mol. Microbiol. 10:867-876(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z17317; CAA78965.1; -; Genomic_DNA.
DR   EMBL; CR382121; CAH02703.1; -; Genomic_DNA.
DR   PIR; S39870; S39870.
DR   RefSeq; XP_451115.1; XM_451115.1.
DR   AlphaFoldDB; P34214; -.
DR   SMR; P34214; -.
DR   STRING; 28985.XP_451115.1; -.
DR   PRIDE; P34214; -.
DR   EnsemblFungi; CAH02703; CAH02703; KLLA0_A02607g.
DR   GeneID; 2896669; -.
DR   KEGG; kla:KLLA0_A02607g; -.
DR   eggNOG; KOG2772; Eukaryota.
DR   HOGENOM; CLU_047470_0_1_1; -.
DR   InParanoid; P34214; -.
DR   OMA; KFGYKTL; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000598; Chromosome A.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..334
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173570"
FT   ACT_SITE        143
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  36477 MW;  DD67646509EE7099 CRC64;
     MSEPSAKKQK FANSLEALKA TGTTVVADTG DFESIAKFTP QDATTNPSLI LAAAKQQAYA
     KLIDSAVQYG KKQGQNIDEQ VEIAVDKLLV EFGTAILKVV PGRVSTEVDA RLSFDKDATV
     KKALEIIKLY EAEGISKDRV LIKIASTWEG IQAAQELEKE HDIHVNLTLL FSFAQAVAAA
     EANVTLISPF VGRILDWYKA STGETYTAET DPGVISVKSI YNYYKKHGYN TIVMGASFRN
     VGEIKALAGV DFLTISPKLL DELLSSDEPV AKILDPESAK AEGSERVSFI NDEPKFRFEL
     NEDAMATEKL SEGIRKFSAD IVTLFDLIKA KIQA