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P26284

- ODPA_RAT

UniProt

P26284 - ODPA_RAT

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Protein
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Gene
Pdha1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Thiamine pyrophosphate By similarity.

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation By similarity.

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: RGD
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: RGD
  2. glucose metabolic process Source: UniProtKB-KW
  3. glycolytic process Source: InterPro
  4. tricarboxylic acid cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC:1.2.4.1)
Alternative name(s):
PDHE1-A type I
Gene namesi
Name:Pdha1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3286. Pdha1.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: RGD
  2. mitochondrion Source: RGD
  3. pyruvate dehydrogenase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion By similarity
Add
BLAST
Chaini30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000020445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-acetyllysine; alternate By similarity
Modified residuei63 – 631N6-succinyllysine; alternate By similarity
Modified residuei232 – 2321Phosphoserine; by PDK11 Publication
Modified residuei244 – 2441N6-acetyllysine; alternate By similarity
Modified residuei244 – 2441N6-succinyllysine; alternate By similarity
Modified residuei267 – 2671N6-acetyllysine By similarity
Modified residuei277 – 2771N6-succinyllysine By similarity
Modified residuei293 – 2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK41 Publication
Modified residuei295 – 2951Phosphoserine By similarity
Modified residuei300 – 3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK41 Publication
Modified residuei301 – 3011Phosphotyrosine By similarity
Modified residuei313 – 3131N6-acetyllysine; alternate By similarity
Modified residuei313 – 3131N6-succinyllysine; alternate By similarity
Modified residuei321 – 3211N6-acetyllysine By similarity
Modified residuei336 – 3361N6-acetyllysine By similarity
Modified residuei385 – 3851N6-succinyllysine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP26284.
PRIDEiP26284.

2D gel databases

World-2DPAGE0004:P26284.

PTM databases

PhosphoSiteiP26284.

Expressioni

Tissue specificityi

In all tissues, but in very low amount in testis.1 Publication

Gene expression databases

GenevestigatoriP26284.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000030279.

Structurei

3D structure databases

ProteinModelPortaliP26284.
SMRiP26284. Positions 29-390.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP26284.
PhylomeDBiP26284.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P26284-1 [UniParc]FASTAAdd to Basket

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MRKMLAAVSR VLAGAAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP    50
PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC 100
CVGLEAGINP TDHLITAYRA HGFTFNRGHA VRAILAELTG RRGGCAKGKG 150
GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN 200
QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP 250
GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 300
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA 350
QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 390
Length:390
Mass (Da):43,227
Last modified:December 12, 2006 - v2
Checksum:i254B5A801E750DC0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101R → H in CAA78146. 1 Publication
Sequence conflicti126 – 1261N → T in CAA78146. 1 Publication
Sequence conflicti129 – 1302HA → LP in CAA78146. 1 Publication
Sequence conflicti134 – 1341I → V1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z12158 mRNA. Translation: CAA78146.1.
PIRiS15891. DERTPA.
S21553. DERTP1.
UniGeneiRn.3655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z12158 mRNA. Translation: CAA78146.1 .
PIRi S15891. DERTPA.
S21553. DERTP1.
UniGenei Rn.3655.

3D structure databases

ProteinModelPortali P26284.
SMRi P26284. Positions 29-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000030279.

Chemistry

ChEMBLi CHEMBL2176823.

PTM databases

PhosphoSitei P26284.

2D gel databases

World-2DPAGE 0004:P26284.

Proteomic databases

PaxDbi P26284.
PRIDEi P26284.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

RGDi 3286. Pdha1.

Phylogenomic databases

eggNOGi COG1071.
HOGENOMi HOG000281336.
HOVERGENi HBG001863.
InParanoidi P26284.
PhylomeDBi P26284.

Gene expression databases

Genevestigatori P26284.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiODPA_RAT
AccessioniPrimary (citable) accession number: P26284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 12, 2006
Last modified: June 11, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

External Data

Dasty 3

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