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   16-JUN-2009, entry version 62.
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; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating 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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- ENZYME REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha
CC       subunit (By similarity).
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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DR   EMBL; Z47812; CAA87793.1; -; Genomic_DNA.
DR   PIR; T24557; T24557.
DR   RefSeq; NP_495693.1; -.
DR   UniGene; Cel.7502; -.
DR   HSSP; P08559; 1NI4.
DR   DIP; DIP:24909N; -.
DR   PRIDE; P52899; -.
DR   Ensembl; T05H10.6; Caenorhabditis elegans.
DR   GeneID; 3565996; -.
DR   KEGG; cel:T05H10.6; -.
DR   WormBase; WBGene00011510; T05H10.6.
DR   WormPep; T05H10.6; CE01643.
DR   BRENDA; 1.2.4.1; 672.
DR   NextBio; 958671; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    397       Probable pyruvate dehydrogenase E1
FT                                component subunit alpha, mitochondrial.
FT                                /FTId=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
//