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P15019 (TAL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [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. HAMAP-Rule MF_00492

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00492

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. HAMAP-Rule MF_00492

Subunit structure

Homodimer.

Miscellaneous

Two isoenzymes seem to be encoded by the same gene.

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

Sequence similarities

Belongs to the transaldolase family. Type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00492
Chain2 – 335334Transaldolase HAMAP-Rule MF_00492
PRO_0000173574

Sites

Active site1441Schiff-base intermediate with substrate Probable

Amino acid modifications

Modified residue21N-acetylserine Ref.7

Experimental info

Sequence conflict2211I → M in CAA34078. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15019 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The ILV5 gene of Saccharomyces cerevisiae is highly expressed."
Petersen J.G.L., Holmberg S.
Nucleic Acids Res. 14:9631-9651(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[5]Harkins H.A., Pringle J.R.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-335.
[6]"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] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[7]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2.
[8]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15953 Genomic DNA. Translation: CAA34078.1.
U19102 Genomic DNA. Translation: AAB67752.1.
X04969 Genomic DNA. Translation: CAA28644.1.
L37016 Genomic DNA. Translation: AAA64519.1.
BK006945 Genomic DNA. Translation: DAA09658.1.
PIRS51462.
RefSeqNP_013458.1. NM_001182243.1.

3D structure databases

ProteinModelPortalP15019.
SMRP15019. Positions 12-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31616. 40 interactions.
DIPDIP-4980N.
IntActP15019. 8 interactions.
MINTMINT-559744.
STRING4932.YLR354C.

2D gel databases

SWISS-2DPAGEP15019.

Proteomic databases

MaxQBP15019.
PaxDbP15019.
PeptideAtlasP15019.
PRIDEP15019.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR354C; YLR354C; YLR354C.
GeneID851068.
KEGGsce:YLR354C.

Organism-specific databases

SGDS000004346. TAL1.

Phylogenomic databases

eggNOGCOG0176.
GeneTreeENSGT00390000017361.
HOGENOMHOG000281234.
KOK00616.
OMAEAKFRWA.
OrthoDBEOG7N905G.

Enzyme and pathway databases

BioCycYEAST:YLR354C-MONOMER.
UniPathwayUPA00115; UER00414.

Gene expression databases

GenevestigatorP15019.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00492. Transaldolase_1.
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERPTHR10683. PTHR10683. 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

NextBio967708.
PROP15019.

Entry information

Entry nameTAL1_YEAST
AccessionPrimary (citable) accession number: P15019
Secondary accession number(s): D6VYZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways