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Q5R490

- ODPA_PONAB

UniProt

Q5R490 - ODPA_PONAB

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Protein
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Gene
PDHA1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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: UniProtKB-EC
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. pyruvate dehydrogenase complex Source: UniProtKB
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_0000020444Add
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 PDK1 By similarity
Modified residuei244 – 2441N6-acetyllysine; alternate By similarity
Modified residuei244 – 2441N6-succinyllysine; alternate By similarity
Modified residuei277 – 2771N6-succinyllysine By similarity
Modified residuei293 – 2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
Modified residuei295 – 2951Phosphoserine By similarity
Modified residuei300 – 3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity
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 By similarity.
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

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.

Structurei

3D structure databases

ProteinModelPortaliQ5R490.
SMRiQ5R490. Positions 29-390.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001863.
InParanoidiQ5R490.
KOiK00161.

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.

Q5R490-1 [UniParc]FASTAAdd to Basket

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MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP    50
PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC 100
CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG 150
GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN 200
QGQIFGAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP 250
GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 300
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA 350
QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 390
Length:390
Mass (Da):43,224
Last modified:December 21, 2004 - v1
Checksum:i4C0A5ADD25CB2D49
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR861366 mRNA. Translation: CAH93426.1.
RefSeqiNP_001127663.1. NM_001134191.1.

Genome annotation databases

GeneIDi100174745.
KEGGipon:100174745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR861366 mRNA. Translation: CAH93426.1 .
RefSeqi NP_001127663.1. NM_001134191.1.

3D structure databases

ProteinModelPortali Q5R490.
SMRi Q5R490. Positions 29-390.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100174745.
KEGGi pon:100174745.

Organism-specific databases

CTDi 5160.

Phylogenomic databases

HOVERGENi HBG001863.
InParanoidi Q5R490.
KOi K00161.

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 German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiODPA_PONAB
AccessioniPrimary (citable) accession number: Q5R490
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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