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P16387 (ODPA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

EC=1.2.4.1
Alternative name(s):
Pyruvate dehydrogenase complex component E1 alpha
Short name=PDHE1-A
Gene names
Name:PDA1
Ordered Locus Names:YER178W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate.

Enzyme regulation

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.

Subunit structure

Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2 beta subunits. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.

Subcellular location

Mitochondrion matrix.

Post-translational modification

Phosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1 (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase phosphatases PTC5 and PTC6. Ref.11

Miscellaneous

Present with 100000 molecules/cell in log phase SD medium.

Sequence caution

The sequence AAB64705.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Ref.1
Chain34 – 420387Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
PRO_0000020452

Amino acid modifications

Modified residue3131Phosphoserine; by PDK1 and PDK2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Experimental info

Sequence conflict761T → S in AAA34847. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16387 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 37019BD9E84D0002

FASTA42046,343
        10         20         30         40         50         60 
MLAASFKRQP SQLVRGLGAV LRTPTRIGHV RTMATLKTTD KKAPEDIEGS DTVQIELPES 

        70         80         90        100        110        120 
SFESYMLEPP DLSYETSKAT LLQMYKDMVI IRRMEMACDA LYKAKKIRGF CHLSVGQEAI 

       130        140        150        160        170        180 
AVGIENAITK LDSIITSYRC HGFTFMRGAS VKAVLAELMG RRAGVSYGKG GSMHLYAPGF 

       190        200        210        220        230        240 
YGGNGIVGAQ VPLGAGLAFA HQYKNEDACS FTLYGDGASN QGQVFESFNM AKLWNLPVVF 

       250        260        270        280        290        300 
CCENNKYGMG TAASRSSAMT EYFKRGQYIP GLKVNGMDIL AVYQASKFAK DWCLSGKGPL 

       310        320        330        340        350        360 
VLEYETYRYG GHSMSDPGTT YRTRDEIQHM RSKNDPIAGL KMHLIDLGIA TEAEVKAYDK 

       370        380        390        400        410        420 
SARKYVDEQV ELADAAPPPE AKLSILFEDV YVKGTETPTL RGRIPEDTWD FKKQGFASRD 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase."
Behal R.H., Browning K.S., Andreed L.J.
Biochem. Biophys. Res. Commun. 164:941-946(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-53 AND 309-322.
[2]"Promoter analysis of the PDA1 gene encoding the E1 alpha subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae."
Wenzel T.J., Zuurmond A.M., Bergmans A., van den Berg J.A., Steensma H.Y.
Yeast 10:297-308(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26109 / X2180.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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.
[5]"DMC1: a meiosis-specific yeast homolog of E. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression."
Bishop D.K., Park D., Xu L., Kleckner N.
Cell 69:439-456(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 335-420.
[6]"Isolation and characterization of a yeast gene that is homologous with a meiosis-specific cDNA from a plant."
Kobayashi T., Hotta Y., Tabata S.
Mol. Gen. Genet. 237:225-232(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-420.
Strain: SK1.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[11]"Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases."
Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.
J. Biol. Chem. 283:9759-9767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-313 BY PKP1/PKP2.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29582 mRNA. Translation: AAA34847.1.
X71664 Genomic DNA. Translation: CAA50657.1.
U18922 Genomic DNA. Translation: AAB64705.1. Different initiation.
M87549 Genomic DNA. Translation: AAA34572.1.
D10865 Genomic DNA. Translation: BAA01636.1.
BK006939 Genomic DNA. Translation: DAA07841.1.
PIRDEBYPA. A36743.
RefSeqNP_011105.4. NM_001179068.3.

3D structure databases

ProteinModelPortalP16387.
SMRP16387. Positions 41-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36931. 214 interactions.
DIPDIP-5117N.
IntActP16387. 15 interactions.
MINTMINT-480200.
STRING4932.YER178W.

Proteomic databases

MaxQBP16387.
PaxDbP16387.
PeptideAtlasP16387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER178W; YER178W; YER178W.
GeneID856925.
KEGGsce:YER178W.

Organism-specific databases

CYGDYER178w.
SGDS000000980. PDA1.

Phylogenomic databases

eggNOGCOG1071.
GeneTreeENSGT00530000063174.
HOGENOMHOG000281336.
KOK00161.
OMARGPNQWI.
OrthoDBEOG7QZGMC.

Enzyme and pathway databases

BioCycYEAST:YER178W-MONOMER.

Gene expression databases

GenevestigatorP16387.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Other

NextBio983395.
PROP16387.

Entry information

Entry nameODPA_YEAST
AccessionPrimary (citable) accession number: P16387
Secondary accession number(s): D3DM87
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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