ID   ODBA_MACFA              Reviewed;         445 AA.
AC   Q8HXY4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE            Short=BCKDH E1-alpha;
DE   Flags: Precursor;
GN   Name=BCKDHA; ORFNames=QccE-11424;
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 branched-chain alpha-keto dehydrogenase complex
CC       catalyzes the overall conversion of alpha-keto acids to acyl-CoA
CC       and CO(2). It contains multiple copies of three enzymatic
CC       components: branched-chain alpha-keto acid decarboxylase (E1),
CC       lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate +
CC       [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
CC       lipoyllysine = [dihydrolipoyllysine-residue (2-
CC       methylpropanoyl)transferase] S-(2-
CC       methylpropanoyl)dihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Heterotetramer of alpha and beta chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- MISCELLANEOUS: Bound potassium ions stabilize the protein
CC       structure (By similarity).
CC   -!- SIMILARITY: Belongs to the BCKDHA family.
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DR   EMBL; AB083305; BAC20584.1; -; mRNA.
DR   HSSP; P12694; 1OLX.
DR   SMR; Q8HXY4; 51-445.
DR   HOVERGEN; Q8HXY4; -.
DR   BRENDA; 1.2.4.4; 3438.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-me...; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   Pfam; PF00676; E1_dh; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Potassium; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     45       Mitochondrion (By similarity).
FT   CHAIN        46    445       2-oxoisovalerate dehydrogenase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000020466.
FT   REGION      157    159       Thiamine pyrophosphate binding (By
FT                                similarity).
FT   METAL       206    206       Potassium (By similarity).
FT   METAL       211    211       Potassium (By similarity).
FT   METAL       212    212       Potassium (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     345    345       Phosphotyrosine (By similarity).
FT   MOD_RES     347    347       Phosphoserine (By similarity).
SQ   SEQUENCE   445 AA;  50538 MW;  AF645FF711238CA4 CRC64;
     MAVAIAAARV WRPNRGLSQA ALLLLWRPGA RGLARSHPHR QQQQFSSLDD KPQFPGASAE
     FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE KVLKLYKSMT LLNTMDRILY
     ESQRQGRISF YMTNYGEEGT HVGSAAALDN TDLVFGQYRE AGVLMYRDYP LELFMAQCYG
     NISDLGKGRQ MPVHYGCKER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA
     ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG
     NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE VNYWDKQDHP
     ISRLRHYLLS QGWWDEEQEK AWRKQSRKKV MKAFEQAERK PKPNPNLLFS DVYQEMPAQL
     RKQQESLARH LQTYGEHYPL EHFDK
//