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TAL1_GIBIN
ID   TAL1_GIBIN              Reviewed;         323 AA.
AC   A0A075DVI9;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Transaldolase {ECO:0000255|PROSITE-ProRule:PRU10019, ECO:0000255|RuleBase:RU000501, ECO:0000303|PubMed:25075521};
DE            EC=2.2.1.2 {ECO:0000255|PROSITE-ProRule:PRU10019, ECO:0000255|RuleBase:RU000501};
DE   AltName: Allergen=Fus p 4.0101 {ECO:0000303|PubMed:25075521};
GN   ORFNames=FPRO05_10296 {ECO:0000312|EMBL:RBA18648.1};
OS   Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=948311 {ECO:0000312|EMBL:AHY02994.1};
RN   [1] {ECO:0000312|EMBL:AHY02994.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC   STRAIN=BCRC 30972 {ECO:0000303|PubMed:25075521};
RX   PubMed=25075521; DOI=10.1371/journal.pone.0103488;
RA   Chou H., Wu K.G., Yeh C.C., Tai H.Y., Tam M.F., Chen Y.S., Shen H.D.;
RT   "The Transaldolase, a Novel Allergen of Fusarium proliferatum, Demonstrates
RT   IgE Cross-Reactivity with Its Human Analogue.";
RL   PLoS ONE 9:E103488-E103488(2014).
RN   [2] {ECO:0000312|EMBL:RBA18648.1, ECO:0000312|Proteomes:UP000251714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 2341 {ECO:0000312|EMBL:RBA18648.1,
RC   ECO:0000312|Proteomes:UP000251714};
RA   Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA   Sreenivasaprasada S.;
RT   "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT   strain ITEM 2341 from Date Palm.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Important for the balance of metabolites in the pentose-
CC       phosphate pathway. Involved in xylose fermentation to ethanol.
CC       {ECO:0000250|UniProtKB:J9MJK9}.
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         ECO:0000255|RuleBase:RU000501};
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:0000255|RuleBase:RU000501}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:J9MJK9}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 47% of
CC       the 17 patients tested allergic to mold F.proliferatum.
CC       {ECO:0000269|PubMed:25075521}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; KF151224; AHY02994.1; -; mRNA.
DR   EMBL; PKMI01000013; RBA18648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075DVI9; -.
DR   SMR; A0A075DVI9; -.
DR   Allergome; 11422; Fus p 4.
DR   Allergome; 11423; Fus p 4.0101.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000251714; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR   GO; GO:0044836; P:D-xylose fermentation; ISS:UniProtKB.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Allergen; Pentose shunt; Schiff base; Transferase.
FT   CHAIN           1..323
FT                   /note="Transaldolase"
FT                   /id="PRO_0000447578"
FT   ACT_SITE        133
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10019"
SQ   SEQUENCE   323 AA;  35535 MW;  156B239A55C15E31 CRC64;
     MSSSLEQLKA TGTTVVSDSG DFVSIGKYKP QDATTNPSLI LAASKKAEYA KLIDVAIDYA
     KQKGGSIDQQ VDDALDRLLV EFGKEILKII PGKVSTEVDA RYSFDTEASV NKALHLIELY
     GEQGISKDRI LIKIAATWEG IKAAEILQRD HGINTNLTLM FSLVQAIGAA EAGAYLISPF
     VGRILDWFKA STKKEYSKEE DPGVQSVKTI FNYYKKYGYN TIVMGASFRN TGEITELAGC
     DYLTISPNLL EDLLNSNEPV PKKLDASQAA SLDIEKKSYI NDEALFRFDF NEDQMAVEKL
     REGISKFAAD AVTLKSILKE KLA
 
 
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