BkdAB

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

Gene name	bkdAB
Synonyms	bfmBAB, bfmB1b, bkd
Essential	no
Product	2-oxoisovalerate dehydrogenase (E1 beta subunit)
Function	utilization of branched-chain keto acids
Gene expression levels in SubtiExpress: bkdAB
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis, Ile, Leu, Val
MW, pI	35 kDa, 4.791
Gene length, protein length	981 bp, 327 aa
Immediate neighbours	bkdB, bkdAA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed 500px

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: BSU24040

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:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: Cytoplasm (Homogeneous) PubMed

Database entries

• Structure:

• UniProt: P37941

• KEGG entry: [3]

• E.C. number: 1.2.4.4

Expression and regulation

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

• Expression browser: bkdAB 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)