BkdAA

• Description: 2-oxoisovalerate dehydrogenase (E1 alpha subunit)
  
  

Gene name	bkdAA
Synonyms	bfmBAA, bfmB1a, bkd
Essential	no
Product	2-oxoisovalerate dehydrogenase (E1 alpha subunit)
Function	utilization of branched-chain keto acids
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis, Ile, Leu, Val
MW, pI	36 kDa, 4.778
Gene length, protein length	990 bp, 330 aa
Immediate neighbours	bkdAB, lpdV
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

BkdR regulon, CodY regulon, SigL regulon

The gene

Basic information

• Locus tag: BSU24050

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO₂ (according to Swiss-Prot)

• Protein family: BCKDHA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: Membrane-proximal (Spotty) PubMed

Database entries

• Structure: 1UMB (from Thermus thermophilus, 42% identity, 57% similarity) PubMed

• UniProt: P37940

• KEGG entry: [3]

• E.C. number: 1.2.4.4

Expression and regulation

• Operon: ptb-bcd-buk-lpdV-bkdAA-bkdAB-bkdB PubMed

• Sigma factor: SigL PubMed

• Regulation:
  • induced in the presence of isoleucine or valine (BkdR) PubMed

• Regulatory mechanism:
  • CodY: transcription repression PubMed
  • BkdR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

M Nickel, G Homuth, C Böhnisch, U Mäder, T Schweder
Cold induction of the Bacillus subtilis bkd operon is mediated by increased mRNA stability.
Mol Genet Genomics: 2004, 272(1);98-107
[PubMed:15241682] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

Tanja Kaan, Georg Homuth, Ulrike Mäder, Julia Bandow, Thomas Schweder
Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.
Microbiology (Reading): 2002, 148(Pt 11);3441-3455
[PubMed:12427936] [WorldCat.org] [DOI] (P p)

M Debarbouille, R Gardan, M Arnaud, G Rapoport
Role of bkdR, a transcriptional activator of the sigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis.
J Bacteriol: 1999, 181(7);2059-66
[PubMed:10094682] [WorldCat.org] [DOI] (P p)

T Kaneda
Iso- and anteiso-fatty acids in bacteria: biosynthesis, function, and taxonomic significance.
Microbiol Rev: 1991, 55(2);288-302
[PubMed:1886522] [WorldCat.org] [DOI] (P p)