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
//