ID   TALDO_CRIGR             Reviewed;         337 AA.
AC   Q8VI73;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2 {ECO:0000250|UniProtKB:P37837};
GN   Name=TALDO1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000312|EMBL:AAL55523.1};
RN   [1] {ECO:0000312|EMBL:AAL55523.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary {ECO:0000312|EMBL:AAL55523.1};
RA   Perl A., Banki K.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the non-oxidative phase
CC       in the pentose phosphate pathway. Catalyzes the reversible conversion
CC       of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC       erythrose-4-phosphate and beta-D-fructose 6-phosphate.
CC       {ECO:0000250|UniProtKB:Q93092}.
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:0000250|UniProtKB:P37837};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17054;
CC         Evidence={ECO:0000250|UniProtKB:P37837};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17055;
CC         Evidence={ECO:0000250|UniProtKB:P37837};
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:0000250|UniProtKB:Q93092}.
CC   -!- SUBUNIT: Homodimer. Interacts with KPNA1 and KPNA4.
CC       {ECO:0000250|UniProtKB:Q93092}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93092}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q93092}. Note=Shuttles between the nucleus and
CC       the cytoplasm. Actively transported into the nucleus in an importin
CC       alpha/beta-dependent manner. Exported into the cytoplasm by CRM1.
CC       {ECO:0000250|UniProtKB:Q93092}.
CC   -!- DOMAIN: The first 10 amino acids are essential for nuclear
CC       localization. {ECO:0000250|UniProtKB:Q93092}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF128242; AAL55523.1; -; mRNA.
DR   AlphaFoldDB; Q8VI73; -.
DR   SMR; Q8VI73; -.
DR   STRING; 10029.NP_001233704.1; -.
DR   eggNOG; KOG2772; Eukaryota.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Pentose shunt; Phosphoprotein;
KW   Schiff base; Transferase.
FT   CHAIN           1..337
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173563"
FT   MOTIF           1..10
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q93092"
FT   ACT_SITE        142
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
FT   MOD_RES         115
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93092"
FT   MOD_RES         219
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
FT   MOD_RES         286
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
FT   MOD_RES         321
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37837"
SQ   SEQUENCE   337 AA;  37386 MW;  B6AED8B21FB1C374 CRC64;
     MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE
     LVEEAIAYGK KLGGPQEEQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
     RAKRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
     AGVTLISPFV GRILDWHVAN TDKKSYEPQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN
     TGEIKALAGC DFLTISPKLL GELLKDNTKL APVLSIKAAQ TSDLGKIHLD EKAFRWLHSE
     DQMAVEKLSD GIRKFAADAI KLERMLTERM FSAENGK