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Reviewed, UniProtKB/Swiss-Prot P15019 (TAL1_YEAST)

Last modified June 16, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transaldolase
    EC=2.2.1.2
Gene names
Name: TAL1
Ordered Locus Names: YLR354C
ORF Names: L9638.6
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.

Subunit structure

Homodimer.

Miscellaneous

Two isoenzymes seem to be encoded by the same gene.

Present with 53000 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPentose shunt
   Molecular functionTransferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpentose-phosphate shunt

Inferred from mutant phenotype. Source: SGD

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

transaldolase activity

Traceable author statement. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 335334Transaldolase
PRO_0000173574

Sites

Active site1441 Ref.5

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue2381Phosphoserine Ref.8

Experimental info

Sequence conflict2211I → M in CAA34078. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15019-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 2A3A96D80E22B157

FASTA33537,036
        10         20         30         40         50         60 
MSEPAQKKQK VANNSLEQLK ASGTVVVADT GDFGSIAKFQ PQDSTTNPSL ILAAAKQPTY 

        70         80         90        100        110        120 
AKLIDVAVEY GKKHGKTTEE QVENAVDRLL VEFGKEILKI VPGRVSTEVD ARLSFDTQAT 

       130        140        150        160        170        180 
IEKARHIIKL FEQEGVSKER VLIKIASTWE GIQAAKELEE KDGIHCNLTL LFSFVQAVAC 

       190        200        210        220        230        240 
AEAQVTLISP FVGRILDWYK SSTGKDYKGE ADPGVISVKK IYNYYKKYGY KTIVMGASFR 

       250        260        270        280        290        300 
STDEIKNLAG VDYLTISPAL LDKLMNSTEP FPRVLDPVSA KKEAGDKISY ISDESKFRFD 

       310        320        330 
LNEDAMATEK LSEGIRKFSA DIVTLFDLIE KKVTA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of the structural gene for yeast transaldolase."
Schaaff I., Hohmann S., Zimmermann F.K.
Eur. J. Biochem. 188:597-603(1990) [PubMed: 2185015] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204510 / AB320.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"The ILV5 gene of Saccharomyces cerevisiae is highly expressed."
Petersen J.G.L., Holmberg S.
Nucleic Acids Res. 14:9631-9651(1986) [PubMed: 3027658] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[4]Harkins H.A., Pringle J.R.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-335.
[5]"Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase."
Miosga T., Schaaff-Gerstenschlaeger I., Franken E., Zimmermann F.K.
Yeast 9:1241-1249(1993) [PubMed: 8109173] [Abstract]
Cited for: ACTIVE SITE.
[6]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract]
Cited for: ACETYLATION AT SER-2.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

X15953 Genomic DNA. Translation: CAA34078.1.
U19102 Genomic DNA. Translation: AAB67752.1.
X04969 Genomic DNA. Translation: CAA28644.1.
L37016 Genomic DNA. Translation: AAA64519.1.
PIRS51462.
RefSeqNP_013458.1.

3D structure databases

HSSPHSSP built from PDB template 1F05 based on UniProtKB P37837.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4980N.
IntActP15019. 15 interactions.

2-D gel databases

SWISS-2DPAGEP15019.

Proteomic databases

PeptideAtlasP15019.

Genome annotation databases

EnsemblYLR354C. Saccharomyces cerevisiae. [Contig view]
GeneID851068.
GenomeReviewsGene locus YLR354C in contig Y13138_GR.
KEGGsce:YLR354C.
NMPDRfig|4932.3.peg.4480.

Organism-specific databases

CYGDYLR354c.
SGDS000004346. TAL1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP15019.
OMAP15019. EYKPQDA.

Enzyme and pathway databases

BRENDA2.2.1.2. 250.

Gene expression databases

GermOnlineYLR354C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_AB.
IPR018225. Transaldolase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR10683. Transaldolase. 1 hit.
PTHR10683:SF3. Transaldolase_AB. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00874. talAB. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio967708.

Entry information

Entry nameTAL1_YEAST
AccessionPrimary (citable) accession number: P15019
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents