ID   TALDO_DICDI             Reviewed;         321 AA.
AC   Q54UP4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Probable transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; ORFNames=DDB_G0280909;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10019};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000039; EAL66996.1; -; Genomic_DNA.
DR   RefSeq; XP_640977.1; XM_635885.1.
DR   AlphaFoldDB; Q54UP4; -.
DR   SMR; Q54UP4; -.
DR   STRING; 44689.DDB0231283; -.
DR   PaxDb; Q54UP4; -.
DR   EnsemblProtists; EAL66996; EAL66996; DDB_G0280909.
DR   GeneID; 8622781; -.
DR   KEGG; ddi:DDB_G0280909; -.
DR   dictyBase; DDB_G0280909; tal.
DR   eggNOG; KOG2772; Eukaryota.
DR   HOGENOM; CLU_047470_0_1_1; -.
DR   InParanoid; Q54UP4; -.
DR   OMA; KFGYKTL; -.
DR   PhylomeDB; Q54UP4; -.
DR   Reactome; R-DDI-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR   Reactome; R-DDI-71336; Pentose phosphate pathway.
DR   UniPathway; UPA00115; UER00414.
DR   PRO; PR:Q54UP4; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; -; 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   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..321
FT                   /note="Probable transaldolase"
FT                   /id="PRO_0000331219"
FT   ACT_SITE        133
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10019"
SQ   SEQUENCE   321 AA;  35523 MW;  9600C46B41D60CE7 CRC64;
     MSNALEELKK YTTVVADTAD FDVLSKYGSQ DSTTNPSLVF QAASDPKYKS LIDDAIKYVN
     AKSGLSEKEK LSLAIDKLFV NFGVEILKIV PGRVSTEVDA RLSYDIDANV KKGRELIALY
     KEAGIDKERV LIKLASTWEG IEAAKILEKE GIHCNLTLLF SLIQAAACAE AQVTLISPFV
     GRITDFYKSK QGVAGFEASK DPGVISVQQI YSYFKKHGYK TSVMGASFRN KEQTIELAGC
     DLLTISPNLL EELKNADASL VTKKLDSTKL PSDIPNKLDV SHSNFLWELN DNEMAYFKTG
     EGIRKFAEDL VKLENQIKKL L