ID   TAL1_FUSO4              Reviewed;         323 AA.
AC   J9MJK9;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Transaldolase;
DE            Short=FoTal;
DE            EC=2.2.1.2;
GN   ORFNames=FOXG_03074;
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   DOI=10.1016/j.procbio.2008.05.013;
RA   Kourtoglou E., Mamma D., Topakas E., Christakopoulos P.;
RT   "Purification, characterization and mass spectrometric sequencing of
RT   transaldolase from Fusarium oxysporum.";
RL   Process Biochem. 43:1094-1101(2008).
CC   -!- FUNCTION: Transaldolase important for the balance of metabolites in the
CC       pentose-phosphate pathway. Involved in xylose fermentation to ethanol.
CC       {ECO:0000269|Ref.2}.
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, ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.49 mM for D-erythrose 4-phosphate {ECO:0000269|Ref.2};
CC         KM=6.66 mM for D-fructose 6-phosphate {ECO:0000269|Ref.2};
CC         Note=kcat is 4114 min(-1) with D-erythrose 4-phosphate as substrate
CC         and 4151 min(-1) with D-fructose 6-phosphate as substrate.;
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|Ref.2};
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: Monomer. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAXH01000183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018236899.1; XM_018380598.1.
DR   AlphaFoldDB; J9MJK9; -.
DR   SMR; J9MJK9; -.
DR   STRING; 426428.J9MJK9; -.
DR   PRIDE; J9MJK9; -.
DR   EnsemblFungi; FOXG_03074T0; FOXG_03074P0; FOXG_03074.
DR   GeneID; 28945221; -.
DR   KEGG; fox:FOXG_03074; -.
DR   VEuPathDB; FungiDB:FOXG_03074; -.
DR   HOGENOM; CLU_047470_0_1_1; -.
DR   OMA; KFGYKTL; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000009097; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004801; F:transaldolase activity; IDA:UniProtKB.
DR   GO; GO:0044836; P:D-xylose fermentation; IDA:UniProtKB.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA: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   Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..323
FT                   /note="Transaldolase"
FT                   /id="PRO_0000430144"
FT   ACT_SITE        133
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10019"
SQ   SEQUENCE   323 AA;  35547 MW;  E206299B536A2B1C CRC64;
     MSSSLEQLKA TGTTVVSDSG DFASIGKYKP QDATTNPSLI LAASKKAEYA KLIDVAIDYA
     KQKGGPIDQQ VDDALDRLLV EFGKEILKII PGKVSTEVDA RYSFDTEASV NKALHLIELY
     GEQGISKDRI LIKIAATWEG IKAAEILQRD HGINTNLTLM FSLVQAIGAA EAGAYLISPF
     VGRILDWFKA STKKEYSKEE DPGVQSVKTI FNYYKKYGYN TIVMGASFRN TGEITELAGC
     DYLTISPNLL EELLNSNEPV PKKLDASQAS SLDIEKKSYI NDEALFRFDF NEDQMAVEKL
     REGISKFAAD AVTLKSILKE KLA