TAL1_YEAST
ID TAL1_YEAST Reviewed; 335 AA.
AC P15019; D6VYZ2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2 {ECO:0000269|PubMed:2185015, ECO:0000269|PubMed:8109173};
GN Name=TAL1; OrderedLocusNames=YLR354C; ORFNames=L9638.6;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=2185015; DOI=10.1111/j.1432-1033.1990.tb15440.x;
RA Schaaff I., Hohmann S., Zimmermann F.K.;
RT "Molecular analysis of the structural gene for yeast transaldolase.";
RL Eur. J. Biochem. 188:597-603(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
RX PubMed=3027658; DOI=10.1093/nar/14.24.9631;
RA Petersen J.G.L., Holmberg S.;
RT "The ILV5 gene of Saccharomyces cerevisiae is highly expressed.";
RL Nucleic Acids Res. 14:9631-9651(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-335.
RA Harkins H.A., Pringle J.R.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=8109173; DOI=10.1002/yea.320091111;
RA Miosga T., Schaaff-Gerstenschlaeger I., Franken E., Zimmermann F.K.;
RT "Lysine144 is essential for the catalytic activity of Saccharomyces
RT cerevisiae transaldolase.";
RL Yeast 9:1241-1249(1993).
RN [7]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000269|PubMed:2185015}.
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:0000269|PubMed:2185015, ECO:0000269|PubMed:8109173};
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:0000305|PubMed:2185015}.
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: Two isoenzymes seem to be encoded by the same gene.
CC {ECO:0000305|PubMed:2185015}.
CC -!- MISCELLANEOUS: Present with 53000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X15953; CAA34078.1; -; Genomic_DNA.
DR EMBL; U19102; AAB67752.1; -; Genomic_DNA.
DR EMBL; X04969; CAA28644.1; -; Genomic_DNA.
DR EMBL; L37016; AAA64519.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09658.1; -; Genomic_DNA.
DR PIR; S51462; S51462.
DR RefSeq; NP_013458.1; NM_001182243.1.
DR AlphaFoldDB; P15019; -.
DR SMR; P15019; -.
DR BioGRID; 31616; 124.
DR DIP; DIP-4980N; -.
DR IntAct; P15019; 17.
DR MINT; P15019; -.
DR STRING; 4932.YLR354C; -.
DR iPTMnet; P15019; -.
DR SWISS-2DPAGE; P15019; -.
DR MaxQB; P15019; -.
DR PaxDb; P15019; -.
DR PRIDE; P15019; -.
DR TopDownProteomics; P15019; -.
DR EnsemblFungi; YLR354C_mRNA; YLR354C; YLR354C.
DR GeneID; 851068; -.
DR KEGG; sce:YLR354C; -.
DR SGD; S000004346; TAL1.
DR VEuPathDB; FungiDB:YLR354C; -.
DR eggNOG; KOG2772; Eukaryota.
DR GeneTree; ENSGT00390000017361; -.
DR HOGENOM; CLU_047470_0_1_1; -.
DR InParanoid; P15019; -.
DR OMA; KFGYKTL; -.
DR BioCyc; YEAST:YLR354C-MON; -.
DR BRENDA; 2.2.1.2; 984.
DR Reactome; R-SCE-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-SCE-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00414.
DR PRO; PR:P15019; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P15019; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004801; F:transaldolase activity; IDA:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IMP:SGD.
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; -; 1.
DR HAMAP; MF_00492; Transaldolase_1; 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 Acetylation; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..335
FT /note="Transaldolase"
FT /id="PRO_0000173574"
FT ACT_SITE 144
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000305|PubMed:8109173"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CONFLICT 221
FT /note="I -> M (in Ref. 1; CAA34078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37036 MW; 2A3A96D80E22B157 CRC64;
MSEPAQKKQK VANNSLEQLK ASGTVVVADT GDFGSIAKFQ PQDSTTNPSL ILAAAKQPTY
AKLIDVAVEY GKKHGKTTEE QVENAVDRLL VEFGKEILKI VPGRVSTEVD ARLSFDTQAT
IEKARHIIKL FEQEGVSKER VLIKIASTWE GIQAAKELEE KDGIHCNLTL LFSFVQAVAC
AEAQVTLISP FVGRILDWYK SSTGKDYKGE ADPGVISVKK IYNYYKKYGY KTIVMGASFR
STDEIKNLAG VDYLTISPAL LDKLMNSTEP FPRVLDPVSA KKEAGDKISY ISDESKFRFD
LNEDAMATEK LSEGIRKFSA DIVTLFDLIE KKVTA
