Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P16387 (ODPA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 141. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Miscellaneous	Present with 100000 molecules/cell in log phase SD medium.
Sequence caution	The sequence AAB64705.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7947791. Source: SGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial nucleoid Inferred from direct assay PubMed 15692048. Source: SGD mitochondrial pyruvate dehydrogenase complex Inferred from direct assay PubMed 2007123. Source: SGD
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from mutant phenotype PubMed 11589696. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 33

Mitochondrion Ref.1

Chain

34 – 420

387

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

PRO_0000020452

Amino acid modifications

Modified residue

254

Phosphoserine Ref.9

Modified residue

309

Phosphotyrosine Ref.14

Modified residue

313

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

315

Phosphoserine Ref.13 Ref.14

Experimental info

Sequence conflict

T → S in AAA34847. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P16387 [UniParc].

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

420

46,343

        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' referencesShow '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. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, MASS SPECTROMETRY. Strain: 2124.
[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].
[9]	"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-254 AND SER-313, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"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, MASS SPECTROMETRY. Strain: ADR376.
[11]	"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, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND SER-315, MASS SPECTROMETRY.
[14]	"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 TYR-309; SER-313 AND SER-315, MASS SPECTROMETRY.
+	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.
PIR	DEBYPA. A36743.
RefSeq	NP_011105.4. NM_001179068.3.
3D structure databases
ProteinModelPortal	P16387.
SMR	P16387. Positions 41-391.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5117N.
IntAct	P16387. 15 interactions.
MINT	MINT-480200.
STRING	4932.YER178W.
Proteomic databases
PaxDb	P16387.
PeptideAtlas	P16387.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER178W; YER178W; YER178W.
GeneID	856925.
KEGG	sce:YER178W. sce:YER182W.
Organism-specific databases
CYGD	YER178w.
SGD	S000000980. PDA1.
Phylogenomic databases
eggNOG	COG1071.
GeneTree	ENSGT00530000063174.
HOGENOM	HOG000281336.
KO	K00161.
OMA	FAQNDPE.
OrthoDB	EOG4DJP51.
Gene expression databases
Genevestigator	P16387.
GermOnline	YER178W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...
Other
NextBio	983395.

Entry information

Entry name

ODPA_YEAST

Accession

Primary (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:	May 1, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents