ID   ODPA_SMIMA              Reviewed;         363 AA.
AC   P52900;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor; Fragment;
GN   Name=PDHA;
OS   Sminthopsis macroura (Stripe-faced dunnart).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sminthopsis.
OX   NCBI_TaxID=9302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=94140363; PubMed=8307573; DOI=10.1016/S0888-7543(05)80366-0;
RA   Fitzgerald J., Wilcox S.A., Graves J.A., Dahl H.-H.M.;
RT   "A eutherian X-linked gene, PDHA1, is autosomal in marsupials: a model
RT   for the evolution of a second, testis-specific variant in eutherian
RT   mammals.";
RL   Genomics 18:636-642(1993).
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.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; L20774; AAA31589.1; -; mRNA.
DR   HSSP; P08559; 1NI4.
DR   SMR; P52900; 2-363.
DR   HOVERGEN; P52900; -.
DR   BRENDA; 1.2.4.1; 293771.
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   2: Evidence at transcript level;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT      <1      2       Mitochondrion (By similarity).
FT   CHAIN         3    363       Pyruvate dehydrogenase E1 component
FT                                subunit alpha, mitochondrial.
FT                                /FTId=PRO_0000020446.
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphotyrosine (By similarity).
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     273    273       Phosphoserine (By similarity).
FT   MOD_RES     274    274       Phosphotyrosine (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   363 AA;  40735 MW;  4884E0A17D7A15A8 CRC64;
     RNFANDATFD IKKCDVHRLE EGPPTTAVLT REEGLKYYKI MQTVRRMELK ADQLYKQKII
     RGFCHLYDGQ EACCMGLEAG INPTDHVITA YRAHGFTYTR GLPVREILAE LTGRRGGCAK
     GKGGSMHMYA KNFYGGNGIV GAQVPLGVGI ALACKYNEKD EICLTLYGDG AANQGQIFEA
     YNMAALWKLP CIFICENNRY GMGTSVERAA ASTDYYKRGD FIPGIMVDGM DVLCVREATK
     FAAAYCRSGK GPMLMELQTY RYHGHSMSDP GVSYRTREEI QEVRSKSDPI MLLKDRMVNN
     NLASIEELKE IDVEVRKEIE DAAQFATADP EPPLEELGYH IYSRDPPFEV RGANQWIKYK
     SVS
//