Pdha1
entrez
18597
canonical
uniprot
P35486
canonical
ensembl
ENSMUSG00000031299
resolver
ensp
ENSMUSP00000033662
resolver
enst
ENSMUST00000033662
resolver
genesymbol
Pdha1
resolver
genesymbol_syn
Pdha-1
resolver
uniprot
Q3UFJ3
resolver
uniprot_entry
ODPA_MOUSE
resolver
uniprot_entry
Q3UFJ3_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation. {ECO:0000250|UniProtKB:P08559}.
uniprot
proteins
amino_acid_sequence
MRKMLAAVSRVLAGSAQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLPVRAILAELTGRRGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATKFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS
uniprot
proteins
ec_number
1.2.4.1
uniprot
proteins
function
FUNCTION: Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex. 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. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (By similarity). 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:11708858, PubMed:20841503). {ECO:0000250|UniProtKB:P08559, ECO:0000269|PubMed:11708858, ECO:0000269|PubMed:20841503}.
uniprot
proteins
mass_dalton
43232
uniprot
proteins
mutagenesis
MUTAGEN 336; /note="K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism."; /evidence="ECO:0000269|PubMed:23835326
uniprot
proteins
post_translational_modification
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. 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). {ECO:0000250|UniProtKB:P26284}.; PTM: Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3. {ECO:0000269|PubMed:19341700, ECO:0000269|PubMed:23835326}.
uniprot
proteins
pubmed
11708858
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1581363
uniprot
proteins
pubmed
17208939
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17314311
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
18586888
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19341700
uniprot
proteins
pubmed
20841503
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
23835326
uniprot
proteins
sequence_length
390
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:19341700}.
uniprot
proteins