ID ODPA_CANLF Reviewed; 13 AA. AC P49823; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, somatic form; DE EC=1.2.4.1; DE AltName: Full=PDHE1-A type I; DE Flags: Fragment; GN Name=PDHA1; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Heart; RX PubMed=9504812; DOI=10.1002/elps.1150181514; RA Dunn M.J., Corbett J.M., Wheeler C.H.; RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog RT heart proteins."; RL Electrophoresis 18:2795-2802(1997). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the CC glycolytic pathway to the tricarboxylic cycle. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)- CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC -!- ACTIVITY REGULATION: Pyruvate dehydrogenase activity is inhibited by CC phosphorylation of PDHA1; it is reactivated by dephosphorylation. CC {ECO:0000250}. CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The CC heterotetramer interacts with DLAT, and is part of the multimeric CC pyruvate dehydrogenase complex that contains multiple copies of CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, CC E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to CC an inner core composed of about 48 DLAT and 12 PDHX molecules (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. CC -!- PTM: Phosphorylation by PDK family kinases inactivates the enzyme; it CC is reactivated by dephosphorylation. {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR InParanoid; P49823; -. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Unplaced. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Unplaced. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:UniProtKB. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:UniProtKB. DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR UCD-2DPAGE; P49823; -. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Direct protein sequencing; Glucose metabolism; KW Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; KW Reference proteome; Thiamine pyrophosphate; Tricarboxylic acid cycle. FT CHAIN 1..>13 FT /note="Pyruvate dehydrogenase E1 component subunit alpha, FT somatic form" FT /id="PRO_0000162214" FT NON_TER 13 SQ SEQUENCE 13 AA; 1513 MW; C97EEBF844085B19 CRC64; XXDATFEIKK XDL //