TAL3_CYBJA
ID TAL3_CYBJA Reviewed; 9 AA.
AC P17441;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 29-SEP-2021, entry version 63.
DE RecName: Full=Transaldolase-3;
DE EC=2.2.1.2;
DE AltName: Full=Transaldolase III;
DE Flags: Fragment;
OS Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=4903;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1092268; DOI=10.1016/0003-9861(75)90495-6;
RA Tsolas O., Sun S.C.;
RT "Isolation of a peptide containing a histidinyl-cysteinyl sequence from the
RT active center of transaldolase.";
RL Arch. Biochem. Biophys. 167:525-533(1975).
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 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 -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR PIR; A11497; A11497.
DR UniPathway; UPA00115; UER00414.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Pentose shunt; Schiff base; Transferase.
FT CHAIN <1..>9
FT /note="Transaldolase-3"
FT /id="PRO_0000173572"
FT NON_TER 1
FT NON_TER 9
SQ SEQUENCE 9 AA; 1033 MW; 325A31A44EB1E058 CRC64;
YGIHCNTLL