Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial precursor

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P26284 (ODPA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. History...

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

Third-party data

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

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
EC=1.2.4.1

Alternative name(s):
PDHE1-A type I

Gene names

Name:

Pdha1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	390 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, and thereby links the glycolytic pathway to the tricarboxylic cycle By similarity.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
Cofactor	Thiamine pyrophosphate By similarity.
Enzyme regulation	Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation By similarity.
Subunit structure	Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules By similarity.
Subcellular location	Mitochondrion matrix Ref.5.
Tissue specificity	In all tissues, but in very low amount in testis. Ref.2
Post-translational modification	Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation 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 7487891. Source: RGD glycolysis Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial pyruvate dehydrogenase complex Traceable author statement Ref.2. Source: RGD
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from direct assay PubMed 7487891. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

Mitochondrion By similarity

Chain

30 – 390

361

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

PRO_0000020445

Amino acid modifications

Modified residue

232

Phosphoserine; by PDK1 Ref.5

Modified residue

289

Phosphotyrosine By similarity

Modified residue

293

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.4 Ref.5

Modified residue

295

Phosphoserine Ref.4

Modified residue

300

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.4 Ref.5

Modified residue

301

Phosphotyrosine Ref.4

Modified residue

321

N6-acetyllysine By similarity

Experimental info

Sequence conflict

R → H in CAA78146. Ref.2

Sequence conflict

126

N → T in CAA78146. Ref.2

Sequence conflict

129 – 130

HA → LP in CAA78146. Ref.2

Sequence conflict

134

I → V Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P26284 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 254B5A801E750DC0
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FASTA

390

43,227

        10         20         30         40         50         60 
MRKMLAAVSR VLAGAAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFNRGHA VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase." Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T. Biochim. Biophys. Acta 1089:1-7(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The pyruvate dehydrogenase complex: cloning of the rat somatic E1 alpha subunit and its coordinate expression with the mRNAs for the E1 beta, E2, and E3 catalytic subunits in developing rat brain." Cullingford T.E., Clark J.B., Phillips I.R. J. Neurochem. 62:1682-1690(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Liver.
[3]	Lubec G., Diao W., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 133-141; 216-226; 245-253; 289-302 AND 324-343, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[4]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295; SER-300 AND TYR-301, MASS SPECTROMETRY. Tissue: Renal collecting duct.
[5]	"Monitoring phosphorylation of the pyruvate dehydrogenase complex." Rardin M.J., Wiley S.E., Naviaux R.K., Murphy A.N., Dixon J.E. Anal. Biochem. 389:157-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-232; SER-293 AND SER-300.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z12158 mRNA. Translation: CAA78146.1.
IPI	IPI00191707.
PIR	DERTPA. S15891. DERTP1. S21553.
UniGene	Rn.3655.
3D structure databases
ProteinModelPortal	P26284.
SMR	P26284. Positions 29-390.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000030279.
PTM databases
PhosphoSite	P26284.
2D gel databases
World-2DPAGE	0004:P26284.
Proteomic databases
PaxDb	P26284.
PRIDE	P26284.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	3286. Pdha1.
Phylogenomic databases
eggNOG	COG1071.
HOGENOM	HOG000281336.
HOVERGEN	HBG001863.
InParanoid	P26284.
OrthoDB	EOG4W0XD6.
Gene expression databases
ArrayExpress	P26284.
Genevestigator	P26284.
GermOnline	ENSRNOG00000025383. Rattus norvegicus.
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...

Entry information

Entry name

ODPA_RAT

Accession

Primary (citable) accession number: P26284

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 12, 2006
Last modified:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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

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

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information