ID   ODPA_PANTR              Reviewed;         390 AA.
AC   A5A6L0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial;
DE            EC=1.2.4.1;
DE   AltName: Full=PDHE1-A type I;
DE   Flags: Precursor;
GN   Name=PDHA1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
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) (By similarity).
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; AB222138; BAF62383.1; -; mRNA.
DR   RefSeq; NP_001104283.1; -.
DR   Ensembl; ENSPTRG00000021717; Pan troglodytes.
DR   GeneID; 465525; -.
DR   KEGG; ptr:465525; -.
DR   BRENDA; 1.2.4.1; 264977.
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     29       Mitochondrion (By similarity).
FT   CHAIN        30    390       Pyruvate dehydrogenase E1 component
FT                                subunit alpha, somatic form,
FT                                mitochondrial.
FT                                /FTId=PRO_0000297491.
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphotyrosine (By similarity).
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphotyrosine (By similarity).
SQ   SEQUENCE   390 AA;  43238 MW;  4F95746CBB792E78 CRC64;
     MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED
     GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA
     HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA
     CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST
     DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS
     YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP
     LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
//