TALDO_PIG
ID TALDO_PIG Reviewed; 337 AA.
AC Q29593; F1RYY6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2 {ECO:0000250|UniProtKB:P37837};
GN Name=TALDO1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|EMBL:CAA23240.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-64.
RC TISSUE=Small intestine {ECO:0000312|EMBL:CAA23240.1};
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
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; F14769; CAA23240.1; -; mRNA.
DR EMBL; AEMK02000006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; F1RYY6; -.
DR PeptideAtlas; Q29593; -.
DR PRIDE; Q29593; -.
DR Ensembl; ENSSSCT00000014042.4; ENSSSCP00000013657.3; ENSSSCG00000012847.4.
DR VGNC; VGNC:100870; TALDO1.
DR eggNOG; KOG2772; Eukaryota.
DR GeneTree; ENSGT00390000017361; -.
DR HOGENOM; CLU_047470_0_1_1; -.
DR OMA; KFGYKTL; -.
DR TreeFam; TF300757; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000012847; Expressed in blood and 43 other tissues.
DR ExpressionAtlas; Q29593; baseline and differential.
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.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Pentose shunt; Phosphoprotein;
KW Reference proteome; Schiff base; Transferase.
FT CHAIN 1..337
FT /note="Transaldolase"
FT /id="PRO_0000173566"
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 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"
FT CONFLICT 57
FT /note="A -> V (in Ref. 2; CAA23240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37418 MW; D4A39D9EE177C8E8 CRC64;
MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE
LVEEALAYGK RLGGSQEEQV TNAVDKLFVL FGAEILKKIP GRVSTEVDAR LSFDRDAMVA
RARRLIELYK EAGVSKDRVL IKLASTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
AGVTLISPFV GRILDWHVAN TDQKSYEPLE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN
TGEIKALAGC DFLTISPQLL GELLKDTSKL VPMLSAKAAQ ASPLEKVHLD EKAFRWLHNE
DRMAVEKLSD GIRKFAADAV KLERMLTERM FSTENGK
