ID   ODBA_PSEPU              Reviewed;         410 AA.
AC   P09060;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE            Short=BCKDH E1-alpha;
GN   Name=bkdA1;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RX   MEDLINE=88329084; PubMed=3416875;
RA   Burns G., Brown T., Hatter K., Idriss J., Sokatch J.R.;
RT   "Similarity of the E1 subunits of branched-chain-oxoacid dehydrogenase
RT   from Pseudomonas putida to the corresponding subunits of mammalian
RT   branched-chain-oxoacid and pyruvate dehydrogenases.";
RL   Eur. J. Biochem. 176:311-317(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC   STRAIN=G2;
RX   MEDLINE=91008935; PubMed=2211503;
RA   Madhusudhan K.T., Huang G., Burns G., Sokatch J.R.;
RT   "Transcriptional analysis of the promoter region of the Pseudomonas
RT   putida branched-chain keto acid dehydrogenase operon.";
RL   J. Bacteriol. 172:5655-5663(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-13.
RX   MEDLINE=96085147; PubMed=8521848;
RA   Hester K., Luo J., Burns G., Braswell E.H., Sokatch J.R.;
RT   "Purification of active E1 alpha 2 beta 2 of Pseudomonas putida
RT   branched-chain-oxoacid dehydrogenase.";
RL   Eur. J. Biochem. 233:828-836(1995).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   MEDLINE=99356017; PubMed=10426958; DOI=10.1038/11563;
RA   Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G.J.;
RT   "Crystal structure of 2-oxoisovalerate and dehydrogenase and the
RT   architecture of 2-oxo acid dehydrogenase multienzyme complexes.";
RL   Nat. Struct. Biol. 6:785-792(1999).
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: Heterodimer of an alpha and a beta chain.
CC   -!- INTERACTION:
CC       P09061:bkdA2; NbExp=1; IntAct=EBI-1027855, EBI-1027848;
CC   -!- SIMILARITY: Belongs to the BCKDHA family.
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DR   EMBL; M57613; AAA65614.1; -; Genomic_DNA.
DR   PIR; S01317; DEPSXA.
DR   PDB; 1QS0; X-ray; 2.40 A; A=2-408.
DR   PDB; 2BP7; X-ray; 2.90 A; A/C/E/G=1-410.
DR   PDBsum; 1QS0; -.
DR   PDBsum; 2BP7; -.
DR   DIP; DIP:6208N; -.
DR   IntAct; P09060; -.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-me...; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DHase_E1.
DR   Pfam; PF00676; E1_dh; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Oxidoreductase;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    410       2-oxoisovalerate dehydrogenase subunit
FT                                alpha.
FT                                /FTId=PRO_0000162249.
FT   HELIX        24     26
FT   HELIX        44     47
FT   HELIX        48     51
FT   HELIX        67     69
FT   HELIX        74     99
FT   STRAND      102    104
FT   TURN        110    112
FT   HELIX       113    122
FT   STRAND      127    130
FT   HELIX       136    141
FT   HELIX       146    154
FT   TURN        160    163
FT   HELIX       173    175
FT   STRAND      182    185
FT   HELIX       186    200
FT   STRAND      207    212
FT   HELIX       214    217
FT   HELIX       219    231
FT   STRAND      235    241
FT   STRAND      243    245
FT   HELIX       250    253
FT   TURN        254    257
FT   HELIX       262    266
FT   STRAND      270    275
FT   HELIX       279    294
FT   STRAND      300    305
FT   HELIX       318    320
FT   HELIX       326    329
FT   HELIX       335    345
FT   HELIX       351    373
FT   STRAND      378    380
FT   HELIX       388    390
FT   STRAND      391    396
FT   HELIX       399    406
SQ   SEQUENCE   410 AA;  45268 MW;  0C998460CCFB9CF4 CRC64;
     MNEYAPLRLH VPEPTGRPGC QTDFSYLRLN DAGQARKPPV DVDAADTADL SYSLVRVLDE
     QGDAQGPWAE DIDPQILRQG MRAMLKTRIF DSRMVVAQRQ KKMSFYMQSL GEEAIGSGQA
     LALNRTDMCF PTYRQQSILM ARDVSLVEMI CQLLSNERDP LKGRQLPIMY SVREAGFFTI
     SGNLATQFVQ AVGWAMASAI KGDTKIASAW IGDGATAESD FHTALTFAHV YRAPVILNVV
     NNQWAISTFQ AIAGGESTTF AGRGVGCGIA SLRVDGNDFV AVYAASRWAA ERARRGLGPS
     LIEWVTYRAG PHSTSDDPSK YRPADDWSHF PLGDPIARLK QHLIKIGHWS EEEHQATTAE
     FEAAVIAAQK EAEQYGTLAN GHIPSAASMF EDVYKEMPDH LRRQRQELGV
//