ID   ODPA_CAEEL              Reviewed;         397 AA.
AC   P52899;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   ORFNames=T05H10.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3).
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         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha subunit.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR   EMBL; Z47812; CAA87793.1; -; Genomic_DNA.
DR   PIR; T24557; T24557.
DR   RefSeq; NP_495693.1; NM_063292.4.
DR   AlphaFoldDB; P52899; -.
DR   SMR; P52899; -.
DR   BioGRID; 533314; 1.
DR   DIP; DIP-24909N; -.
DR   IntAct; P52899; 1.
DR   STRING; 6239.T05H10.6b; -.
DR   EPD; P52899; -.
DR   PaxDb; P52899; -.
DR   PeptideAtlas; P52899; -.
DR   PRIDE; P52899; -.
DR   EnsemblMetazoa; T05H10.6a.1; T05H10.6a.1; WBGene00011510.
DR   EnsemblMetazoa; T05H10.6a.2; T05H10.6a.2; WBGene00011510.
DR   EnsemblMetazoa; T05H10.6a.3; T05H10.6a.3; WBGene00011510.
DR   GeneID; 3565996; -.
DR   UCSC; T05H10.6b; c. elegans.
DR   CTD; 3565996; -.
DR   WormBase; T05H10.6a; CE01643; WBGene00011510; -.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   InParanoid; P52899; -.
DR   Reactome; R-CEL-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-CEL-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-CEL-70268; Pyruvate metabolism.
DR   PRO; PR:P52899; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011510; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; P52899; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW   Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..397
FT                   /note="Probable pyruvate dehydrogenase E1 component subunit
FT                   alpha, mitochondrial"
FT                   /id="PRO_0000020439"
SQ   SEQUENCE   397 AA;  43792 MW;  27FB6410B0EA8513 CRC64;
     MSLFARQLQS LTASGIRTQQ VRLASTEVSF HTKPCKLHKL DNGPNTSVTL NREDALKYYR
     DMQVIRRMES AAGNLYKEKK IRGFCHLYSG QEACAVGMKA AMTEGDAVIT AYRCHGWTWL
     LGATVTEVLA ELTGRVAGNV HGKGGSMHMY TKNFYGGNGI VGAQQPLGAG VALAMKYREQ
     KNVCVTLYGD GAANQGQLFE ATNMAKLWDL PVLFVCENNG FGMGTTAERS SASTEYYTRG
     DYVPGIWVDG MDILAVREAT KWAKEYCDSG KGPLMMEMAT YRYHGHSMSD PGTSYRTREE
     IQEVRKTRDP ITGFKDRIIT SSLATEEELK AIDKEVRKEV DEALKIATSD GVLPPEALYA
     DIYHNTPAQE IRGATIDETI VQPFKTSADV LKSIGRA