ID Q0UEY2_PHANO Unreviewed; 344 AA.
AC Q0UEY2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
GN ORFNames=SNOG_09682 {ECO:0000313|EMBL:EAT82947.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT82947.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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|ARBA:ARBA00004857,
CC ECO:0000256|RuleBase:RU000501}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012}.
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DR EMBL; CH445339; EAT82947.2; -; Genomic_DNA.
DR RefSeq; XP_001799969.1; XM_001799917.1.
DR AlphaFoldDB; Q0UEY2; -.
DR STRING; 321614.Q0UEY2; -.
DR EnsemblFungi; SNOT_09682; SNOT_09682; SNOG_09682.
DR GeneID; 5976874; -.
DR KEGG; pno:SNOG_09682; -.
DR VEuPathDB; FungiDB:JI435_096820; -.
DR eggNOG; KOG2772; Eukaryota.
DR HOGENOM; CLU_047470_0_1_1; -.
DR InParanoid; Q0UEY2; -.
DR OrthoDB; 1972468at2759; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR NCBIfam; TIGR00874; talAB; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU000501};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000501}.
SQ SEQUENCE 344 AA; 37424 MW; 3A72BC1C7B42F3C0 CRC64;
MSSSLDQLKA TGTVSAPPSF TASELPEMSP VVVCDSGDFA TIAKYQPQDA TTNPSLILAA
SKKEEYAKLI DSAVEYGKKH GGSNIEDQVD ATLDNLLVQF GKEILKIIPG KVSTEVDARF
SFDTEASVTK ALRIIDLYKE QGIGKERILI KIASTWEGIK AAEILQSKHG INTNLTLMFS
QTQAIAAAEA GAFLISPFVG RILDWYKAST KNGVHQGGGL PVSRASRNIL QLLTRSSGYK
TIVMGASFRS IGEVTELAGC DYLTIAPNLL EQLYNSQDPV PKKLDASGAN SLDLEKKTYI
NNEAEFRFYF NEDQMAVEKL REGISKFAAD AVTLKDILRQ KIQA
//
