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Protein

Transaldolase

Gene

TAL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441Schiff-base intermediate with substrate1 Publication

GO - Molecular functioni

  1. sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Source: SGD

GO - Biological processi

  1. pentose-phosphate shunt Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pentose shunt

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciYEAST:YLR354C-MONOMER.
ReactomeiREACT_233695. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_251001. Insulin effects increased synthesis of Xylulose-5-Phosphate.
UniPathwayiUPA00115; UER00414.

Names & Taxonomyi

Protein namesi
Recommended name:
Transaldolase (EC:2.2.1.2)
Gene namesi
Name:TAL1
Ordered Locus Names:YLR354C
ORF Names:L9638.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000004346. TAL1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 335334TransaldolasePRO_0000173574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP15019.
PaxDbiP15019.
PeptideAtlasiP15019.
PRIDEiP15019.

2D gel databases

SWISS-2DPAGEP15019.

Expressioni

Gene expression databases

GenevestigatoriP15019.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi31616. 42 interactions.
DIPiDIP-4980N.
IntActiP15019. 8 interactions.
MINTiMINT-559744.
STRINGi4932.YLR354C.

Structurei

3D structure databases

ProteinModelPortaliP15019.
SMRiP15019. Positions 12-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transaldolase family. Type 1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0176.
GeneTreeiENSGT00390000017361.
HOGENOMiHOG000281234.
InParanoidiP15019.
KOiK00616.
OMAiFNAIDEY.
OrthoDBiEOG7N905G.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00492. Transaldolase_1.
InterProiIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15019-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEPAQKKQK VANNSLEQLK ASGTVVVADT GDFGSIAKFQ PQDSTTNPSL
60 70 80 90 100
ILAAAKQPTY AKLIDVAVEY GKKHGKTTEE QVENAVDRLL VEFGKEILKI
110 120 130 140 150
VPGRVSTEVD ARLSFDTQAT IEKARHIIKL FEQEGVSKER VLIKIASTWE
160 170 180 190 200
GIQAAKELEE KDGIHCNLTL LFSFVQAVAC AEAQVTLISP FVGRILDWYK
210 220 230 240 250
SSTGKDYKGE ADPGVISVKK IYNYYKKYGY KTIVMGASFR STDEIKNLAG
260 270 280 290 300
VDYLTISPAL LDKLMNSTEP FPRVLDPVSA KKEAGDKISY ISDESKFRFD
310 320 330
LNEDAMATEK LSEGIRKFSA DIVTLFDLIE KKVTA
Length:335
Mass (Da):37,036
Last modified:January 23, 2007 - v4
Checksum:i2A3A96D80E22B157
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211I → M in CAA34078. (PubMed:2185015)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS51462.
RefSeqiNP_013458.1. NM_001182243.1.

Genome annotation databases

EnsemblFungiiYLR354C; YLR354C; YLR354C.
GeneIDi851068.
KEGGisce:YLR354C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS51462.
RefSeqiNP_013458.1. NM_001182243.1.

3D structure databases

ProteinModelPortaliP15019.
SMRiP15019. Positions 12-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31616. 42 interactions.
DIPiDIP-4980N.
IntActiP15019. 8 interactions.
MINTiMINT-559744.
STRINGi4932.YLR354C.

2D gel databases

SWISS-2DPAGEP15019.

Proteomic databases

MaxQBiP15019.
PaxDbiP15019.
PeptideAtlasiP15019.
PRIDEiP15019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR354C; YLR354C; YLR354C.
GeneIDi851068.
KEGGisce:YLR354C.

Organism-specific databases

SGDiS000004346. TAL1.

Phylogenomic databases

eggNOGiCOG0176.
GeneTreeiENSGT00390000017361.
HOGENOMiHOG000281234.
InParanoidiP15019.
KOiK00616.
OMAiFNAIDEY.
OrthoDBiEOG7N905G.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00414.
BioCyciYEAST:YLR354C-MONOMER.
ReactomeiREACT_233695. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_251001. Insulin effects increased synthesis of Xylulose-5-Phosphate.

Miscellaneous databases

NextBioi967708.
PROiP15019.

Gene expression databases

GenevestigatoriP15019.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00492. Transaldolase_1.
InterProiIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR004730. Transaldolase_1.
IPR018225. Transaldolase_AS.
[Graphical view]
PANTHERiPTHR10683. PTHR10683. 1 hit.
PfamiPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00874. talAB. 1 hit.
PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTAL1_YEAST
AccessioniPrimary (citable) accession number: P15019
Secondary accession number(s): D6VYZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Two isoenzymes seem to be encoded by the same gene.
Present with 53000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.