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Details on Person UniProt:P08559 PDHA1

Class:Id	ReferenceGeneProduct:60874
_chainChangeLog	transit peptide:1-30 added on Sat February 7 2015;chain:31-390 added on Sat February 7 2015;transit peptide:1-30 for 60874 removed on Fri May 15 2020;chain:31-390 for 60874 removed on Fri May 15 2020;transit peptide:1-29 for 60874 added on Fri May 15 2020;chain:30-390 for 60874 added on Fri May 15 2020
_displayName	UniProt:P08559 PDHA1
_timestamp	2026-02-20 21:42:29
chain	transit peptide:1-29 chain:30-390
checksum	4D685BBE44A92D4B
comment	FUNCTION Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex (PubMed:17474719, PubMed:19081061). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (PubMed:19081061, PubMed:7782287). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed:17474719, PubMed:19081061, PubMed:7782287).CATALYTIC ACTIVITY N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2COFACTOR Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.BIOPHYSICOCHEMICAL PROPERTIES Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase (PDH) 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.INTERACTION Ubiquitous.PTM 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. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.PTM Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).DISEASE The disease is caused by variants affecting the gene represented in this entry.SEQUENCE CAUTION Extended N-terminus.
description	recommendedName: fullName evidence="34"Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial ecNumber evidence="10 11 20"1.2.4.1 alternativeName: PDHE1-A type I
geneName	PDHA1 PHE1A
identifier	P08559
isSequenceChanged	FALSE
keyword	3D-structure Acetylation Alternative splicing Carbohydrate metabolism Direct protein sequencing Disease variant Glucose metabolism Leigh syndrome Magnesium Metal-binding Mitochondrion Oxidoreductase Phosphoprotein Primary mitochondrial disease Proteomics identification Pyruvate Reference proteome Thiamine pyrophosphate Transit peptide Tricarboxylic acid cycle
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	PDHA1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8988547] ENSEMBL:ENSG00000131828 PDHA1 [Homo sapiens]
secondaryIdentifier	ODPA_HUMAN A5YVE9 B2R5P7 B7Z3T7 B7Z3X5 Q53H41 Q5JPT8 Q9NP12 Q9UBJ8 Q9UBU0 Q9UNG4 Q9UNG5
sequenceLength	390
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:8968905] UniProt:P08559-1 PDHA1 [Homo sapiens] [ReferenceIsoform:8968906] UniProt:P08559-2 PDHA1 [Homo sapiens] [ReferenceIsoform:8968907] UniProt:P08559-3 PDHA1 [Homo sapiens] [ReferenceIsoform:8968908] UniProt:P08559-4 PDHA1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:69966] PDHA1 [mitochondrial matrix] [Homo sapiens] [EntityWithAccessionedSequence:204161] p-S293,S300-PDHA1 [mitochondrial matrix] [Homo sapiens]
(referenceSequence)	[ModifiedResidue:210330] O-phospho-L-serine at 293 [ModifiedResidue:210338] O-phospho-L-serine at 300
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No pathways have been reviewed or authored by UniProt:P08559 PDHA1 (60874)