ID   ODPA_MACFA              Reviewed;         390 AA.
AC   Q8HXW9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 38.
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; ORFNames=QccE-20080;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological
RT   disease genes.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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; AB083322; BAC20601.1; -; mRNA.
DR   HSSP; P08559; 1NI4.
DR   SMR; Q8HXW9; 29-390.
DR   HOVERGEN; Q8HXW9; -.
DR   BRENDA; 1.2.4.1; 3438.
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_0000020441.
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;  43366 MW;  420CE38364BDB33C CRC64;
     MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED
     GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA
     HGFTFTRGLS VREILAELTG RKGGCAKGKG GSTHMYAKNF YRGNGIVGAQ VPLGAGIALA
     CKYNGKDEVC LTLYGDGAAD QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST
     DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
     YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP
     LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
//