ID   ODBB_PSEAE              Reviewed;         350 AA.
AC   Q9I1M1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit beta;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE            Short=BCKDH E1-beta;
GN   Name=bkdA2; OrderedLocusNames=PA2248;
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}.
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DR   EMBL; AE004091; AAG05636.1; -; Genomic_DNA.
DR   PIR; D83365; D83365.
DR   PIR; S63478; S63478.
DR   RefSeq; NP_250938.1; NC_002516.2.
DR   RefSeq; WP_003089248.1; NZ_QZGE01000014.1.
DR   AlphaFoldDB; Q9I1M1; -.
DR   SMR; Q9I1M1; -.
DR   STRING; 287.DR97_6302; -.
DR   PaxDb; Q9I1M1; -.
DR   PRIDE; Q9I1M1; -.
DR   EnsemblBacteria; AAG05636; AAG05636; PA2248.
DR   GeneID; 879226; -.
DR   KEGG; pae:PA2248; -.
DR   PATRIC; fig|208964.12.peg.2349; -.
DR   PseudoCAP; PA2248; -.
DR   HOGENOM; CLU_012907_1_0_6; -.
DR   InParanoid; Q9I1M1; -.
DR   OMA; SEAYYMA; -.
DR   PhylomeDB; Q9I1M1; -.
DR   BioCyc; PAER208964:G1FZ6-2287-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   GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..350
FT                   /note="2-oxoisovalerate dehydrogenase subunit beta"
FT                   /id="PRO_0000287783"
SQ   SEQUENCE   350 AA;  38325 MW;  D7983A05A9B3EB0A CRC64;
     MNAMNPQHEN AQTVTSMTMI QALRSAMDIM LERDDDVVVF GQDVGYFGGV FRCTEGLQKK
     YGTSRVFDAP ISESGIIGAA VGMGAYGLRP VVEIQFADYV YPASDQLISE AARLRYRSAG
     DFIVPMTVRM PCGGGIYGGQ THSQSPEAMF TQVCGLRTVM PSNPYDAKGL LIACIENDDP
     VIFLEPKRLY NGPFDGHHDR PVTPWSKHPA SQVPDGYYKV PLDKAAIVRP GAALTVLTYG
     TMVYVAQAAA DETGLDAEII DLRSLWPLDL ETIVASVKKT GRCVIAHEAT RTCGFGAELM
     SLVQEHCFHH LEAPIERVTG WDTPYPHAQE WAYFPGPARV GAAFKRVMEV