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   25-MAY-2022, entry version 66.
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; 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}.
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DR   UCD-2DPAGE; P49823; -.
DR   Proteomes; UP000002254; 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.
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