ID   ODBA_PSEAE              Reviewed;         410 AA.
AC   Q9I1M2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
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; OrderedLocusNames=PA2247;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC       the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: branched-chain
CC       alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC         methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC         N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
CC         Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG05635.1; -; Genomic_DNA.
DR   PIR; C83365; C83365.
DR   PIR; S05057; S05057.
DR   RefSeq; NP_250937.1; NC_002516.2.
DR   RefSeq; WP_003111886.1; NZ_QZGE01000014.1.
DR   AlphaFoldDB; Q9I1M2; -.
DR   SMR; Q9I1M2; -.
DR   STRING; 287.DR97_6303; -.
DR   PaxDb; Q9I1M2; -.
DR   PRIDE; Q9I1M2; -.
DR   EnsemblBacteria; AAG05635; AAG05635; PA2247.
DR   GeneID; 877901; -.
DR   KEGG; pae:PA2247; -.
DR   PATRIC; fig|208964.12.peg.2348; -.
DR   PseudoCAP; PA2247; -.
DR   HOGENOM; CLU_029393_1_0_6; -.
DR   InParanoid; Q9I1M2; -.
DR   OMA; DWHTGYD; -.
DR   PhylomeDB; Q9I1M2; -.
DR   BioCyc; PAER208964:G1FZ6-2286-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR   InterPro; IPR034616; BCKDH_E1-a.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR022593; Oxoisoval_DH_suAlpha_N_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF12573; OxoDH_E1alpha_N; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..410
FT                   /note="2-oxoisovalerate dehydrogenase subunit alpha"
FT                   /id="PRO_0000287782"
SQ   SEQUENCE   410 AA;  45256 MW;  BE3AF6FAB66F0F01 CRC64;
     MSDYEPLRLH VPEPTGRPGC KTDFSYLHLS PAGEVRKPPV DVEPAETSDL AYSLVRVLDD
     DGHAVGPWNP QLSNEQLLRG MRAMLKTRLF DARMLTAQRQ KKLSFYMQCL GEEAIATAHT
     LALRDGDMCF PTYRQQGILI TREYPLVDMI CQLLSNEADP LKGRQLPIMY SSKEAGFFSI
     SGNLATQFIQ AVGWGMASAI KGDTRIASAW IGDGATAESD FHTALTFAHV YRAPVILNVV
     NNQWAISTFQ AIAGGEGTTF ANRGVGCGIA SLRVDGNDFL AVYAASEWAA ERARRNLGPS
     LIEWVTYRAG PHSTSDDPSK YRPADDWTNF PLGDPIARLK RHMIGLGIWS EEQHEATHKA
     LEAEVLAAQK QAESHGTLID GRVPSAASMF EDVYAELPEH LRRQRQELGV