ID   TALDO_BOVIN             Reviewed;         337 AA.
AC   Q2TBL6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=TALDO1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC109965; AAI09966.1; -; mRNA.
DR   RefSeq; NP_001030360.2; NM_001035283.2.
DR   AlphaFoldDB; Q2TBL6; -.
DR   SMR; Q2TBL6; -.
DR   STRING; 9913.ENSBTAP00000013650; -.
DR   PaxDb; Q2TBL6; -.
DR   PeptideAtlas; Q2TBL6; -.
DR   PRIDE; Q2TBL6; -.
DR   GeneID; 513453; -.
DR   KEGG; bta:513453; -.
DR   CTD; 6888; -.
DR   eggNOG; KOG2772; Eukaryota.
DR   InParanoid; Q2TBL6; -.
DR   OrthoDB; 1402459at2759; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Pentose shunt; Phosphoprotein; Reference proteome;
KW   Schiff base; Transferase.
FT   CHAIN           1..337
FT                   /note="Transaldolase"
FT                   /id="PRO_0000246173"
FT   ACT_SITE        142
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
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;  37685 MW;  5CE56272B7706242 CRC64;
     MSGSPVKRQR MENALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPTYQE
     LVEEAIAYGR KLGGSQEEQI TNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
     RARRLIELYK EAGISKERIL IKLSSTWEGI QAGKELEEHH GIRCNMTLLF SFAQAVACAE
     AGVTLISPFV GRILDWHVAN TDKKSYETQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN
     TGEIKALAGC DFLTISPQLL GELLKDHSKL TPVLSAKAAQ ASDLEKIQLD EKAFRWLHNE
     DRMAVEKLSD GIRRFAADAV KLERMLRERM FSAENGK