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Database: UniProt
Entry: F9FYD6_FUSOF
LinkDB: F9FYD6_FUSOF
Original site: F9FYD6_FUSOF 
ID   F9FYD6_FUSOF            Unreviewed;       336 AA.
AC   F9FYD6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Transaldolase {ECO:0000256|RuleBase:RU000501};
DE            EC=2.2.1.2 {ECO:0000256|RuleBase:RU000501};
GN   ORFNames=FOXB_11418 {ECO:0000313|EMBL:EGU78074.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU78074.1};
RN   [1] {ECO:0000313|EMBL:EGU78074.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU78074.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:0000256|RuleBase:RU000501}.
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:0000256|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:0000256|RuleBase:RU000501}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU78074.1}.
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DR   EMBL; AFQF01002878; EGU78074.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FYD6; -.
DR   STRING; 660025.F9FYD6; -.
DR   PaxDb; 5507-FOXG_15418P0; -.
DR   UniPathway; UPA00115; UER00414.
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   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF34; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   4: Predicted;
KW   Pentose shunt {ECO:0000256|RuleBase:RU000501};
KW   Transferase {ECO:0000256|RuleBase:RU000501}.
SQ   SEQUENCE   336 AA;  37142 MW;  46C56240F8B05CC9 CRC64;
     MTTLLDALRQ TSRVDCDTLD SNVPHELGPF VDCTSNQVSV LSKPVSPSSA DLLQAIAFSE
     ISRPLAGEPL LHHDALIREA IQSARGALKD LQGSATFEEF VVQILTNPKL SYSTNGTISD
     AYRIVNIFKH LAPDFDEKRV CIKIPATWEG LQACRTLEMK GIATLATTMF CMEQAALAAE
     AQCTYIAPYV NELKVHFEAG YVDENKAFEF CREAQAYYVS HSFRTQVLAA SLTSVDEVMQ
     LAGIQHVTIS PNLLNGLAAA DLSTWNGKLG EYFAQGLAKK SWEMKDYNAL VRDESSWRMA
     FTRSGFGTSE GKIIQAINYF ADFQDKFEEL VKQHAG
//
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