ID   ODBA_BOVIN              Reviewed;         455 AA.
AC   P11178;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JUN-2009, entry version 73.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88243770; PubMed=3379058;
RA   Hu C.-W.C., Lau K.S., Griffin T.A., Chuang J.L., Fisher C.W.,
RA   Cox R.P., Chuang D.T.;
RT   "Isolation and sequencing of a cDNA encoding the decarboxylase
RT   (E1)alpha precursor of bovine branched-chain alpha-keto acid
RT   dehydrogenase complex. Expression of E1 alpha mRNA and subunit in
RT   maple-syrup-urine-disease and 3T3-L1 cells.";
RL   J. Biol. Chem. 263:9007-9014(1988).
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.
CC   -!- SUBUNIT: Heterotetramer of alpha and beta chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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; J03759; AAA30595.1; -; mRNA.
DR   IPI; IPI00715308; -.
DR   PIR; A28073; DEBOXA.
DR   RefSeq; NP_776931.1; -.
DR   UniGene; Bt.5287; -.
DR   HSSP; P12694; 1DTW.
DR   SMR; P11178; 61-455.
DR   Ensembl; ENSBTAG00000016037; Bos taurus.
DR   GeneID; 282149; -.
DR   KEGG; bta:282149; -.
DR   HOVERGEN; P11178; -.
DR   BRENDA; 1.2.4.4; 251.
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     55       Mitochondrion.
FT   CHAIN        56    455       2-oxoisovalerate dehydrogenase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000020464.
FT   REGION      167    169       Thiamine pyrophosphate binding (By
FT                                similarity).
FT   METAL       216    216       Potassium (By similarity).
FT   METAL       221    221       Potassium (By similarity).
FT   METAL       222    222       Potassium (By similarity).
FT   MOD_RES     347    347       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphotyrosine (By similarity).
FT   MOD_RES     357    357       Phosphoserine (By similarity).
SQ   SEQUENCE   455 AA;  51678 MW;  66A7CA6003E0B846 CRC64;
     MQGSAKMAMA VAVAVARVWR PSRGLGRTGL PLLRLLGARG LARFHPHRWQ QQQHFSSLDD
     KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPQE KVLKFYKSMT
     LLNTMDRILY ESQRQGRISF YMTNYGEEGT HVGSAAALDD TDLVFGQYRE AGVLMYRDYP
     LELFMAQCYG NVSDLGKGRQ MPVHYGCRER HFVTISSPLA TQIPQAVGAA YAAKRANANR
     VVICYFGEGA ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG
     YGILSIRVDG NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE
     VNYWDKQDHP ISRLRHHLQS RGWWDDEQEK AWRKQSRKKV MEAFEQAERK LKPNPSLIFS
     DVYQEMPAQL RKQQESLARH LQTYGEHYPL DHFEK
//