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P26284 (ODPA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

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

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length390 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, 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.4.

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.

Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000020445

Amino acid modifications

Modified residue631N6-acetyllysine; alternate By similarity
Modified residue631N6-succinyllysine; alternate By similarity
Modified residue2321Phosphoserine; by PDK1 Ref.4
Modified residue2441N6-acetyllysine; alternate By similarity
Modified residue2441N6-succinyllysine; alternate By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue2771N6-succinyllysine By similarity
Modified residue2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.4
Modified residue2951Phosphoserine By similarity
Modified residue3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.4
Modified residue3011Phosphotyrosine By similarity
Modified residue3131N6-acetyllysine; alternate By similarity
Modified residue3131N6-succinyllysine; alternate By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue3361N6-acetyllysine By similarity
Modified residue3851N6-succinyllysine By similarity

Experimental info

Sequence conflict101R → H in CAA78146. Ref.2
Sequence conflict1261N → T in CAA78146. Ref.2
Sequence conflict129 – 1302HA → LP in CAA78146. Ref.2
Sequence conflict1341I → V Ref.1

Sequences

Sequence LengthMass (Da)Tools
P26284 [UniParc].

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

FASTA39043,227
        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

[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, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"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.
PIRDERTPA. S15891.
DERTP1. S21553.
UniGeneRn.3655.

3D structure databases

ProteinModelPortalP26284.
SMRP26284. Positions 29-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000030279.

Chemistry

ChEMBLCHEMBL2176823.

PTM databases

PhosphoSiteP26284.

2D gel databases

World-2DPAGE0004:P26284.

Proteomic databases

PaxDbP26284.
PRIDEP26284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD3286. Pdha1.

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281336.
HOVERGENHBG001863.
InParanoidP26284.
PhylomeDBP26284.

Gene expression databases

GenevestigatorP26284.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_RAT
AccessionPrimary (citable) accession number: P26284
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program