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Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.1 Publication

Cofactori

thiamine diphosphate1 Publication

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.1 Publication

GO - Molecular functioni

GO - Biological processi

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1 – 28MitochondrionBy similarityAdd BLAST›28
ChainiPRO_000002044329 – 389Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei62N6-acetyllysine; alternateBy similarity1
Modified residuei62N6-succinyllysine; alternateBy similarity1
Modified residuei230PhosphothreonineBy similarity1
Modified residuei231Phosphoserine; by PDK1By similarity1
Modified residuei243N6-acetyllysine; alternateBy similarity1
Modified residuei243N6-succinyllysine; alternateBy similarity1
Modified residuei276N6-succinyllysineBy similarity1
Modified residuei292Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity1
Modified residuei294PhosphoserineBy similarity1
Modified residuei299Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity1
Modified residuei300PhosphotyrosineBy similarity1
Modified residuei312N6-acetyllysine; alternateBy similarity1
Modified residuei312N6-succinyllysine; alternateBy similarity1
Modified residuei320N6-acetyllysineBy similarity1
Modified residuei335N6-acetyllysineBy similarity1
Modified residuei384N6-succinyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Ser-231, Ser-292 and Ser-299 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-292 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-231, Ser-292 and Ser-299, is required for reactivation.1 Publication
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP29804.
PeptideAtlasiP29804.
PRIDEiP29804.

PTM databases

iPTMnetiP29804.

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).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021757.

Structurei

3D structure databases

ProteinModelPortaliP29804.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0225. Eukaryota.
COG1071. LUCA.
HOVERGENiHBG001863.
InParanoidiP29804.

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: Fragment.

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

P29804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GKMLAAVSRV LSGVAQKPAS RVLVASRTFA NDATFEIKKC DLHRLEEGPP
60 70 80 90 100
VTTVLTREDG LKYYRMMQTV RRMELKADQL YKQKIIRGFC HLCDGQEACC
110 120 130 140 150
VGLEAGINPT DHLITAYRAH GFTFTRGLSV REILAELTGR RGGCGKGKGG
160 170 180 190 200
SMHMYAKNFY GGNGIVGAQV PLGAGIALAC KYNGKDEVCL TLYGDGAANQ
210 220 230 240 250
GQIFEAYNMA ALWKLPCVFI CENNRYGMGT SVERAAASTD YYKRGDFIPG
260 270 280 290 300
LRVDGMDILC VREATRFAAA YCRSGKGPIL MELQTYRYHG HSMSDPGVSY
310 320 330 340 350
RTREEIQEVR SKSDPIMLLK DRMVNSNLAS VEELKEIDVE VRKEIEDAAQ
360 370 380
FATADPEPPL EELGYHIYCN DPPFEVRGAN QWIKFKSIS
Length:389
Mass (Da):43,121
Last modified:April 1, 1993 - v1
Checksum:iE9C7DF85389A9A47
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52990 mRNA. Translation: CAA37180.1.
PIRiS20813. DEPGPA.
UniGeneiSsc.50287.
Ssc.98154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52990 mRNA. Translation: CAA37180.1.
PIRiS20813. DEPGPA.
UniGeneiSsc.50287.
Ssc.98154.

3D structure databases

ProteinModelPortaliP29804.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021757.

PTM databases

iPTMnetiP29804.

Proteomic databases

PaxDbiP29804.
PeptideAtlasiP29804.
PRIDEiP29804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0225. Eukaryota.
COG1071. LUCA.
HOVERGENiHBG001863.
InParanoidiP29804.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiODPA_PIG
AccessioniPrimary (citable) accession number: P29804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 5, 2016
This is version 93 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.