BkdAA

From SubtiWiki
Revision as of 16:58, 22 June 2009 by CLammers (talk | contribs)
Jump to: navigation, search
  • 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:
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
BkdAA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU24050

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:
  • Swiss prot entry:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

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)

Tanja Kaan, Georg Homuth, Ulrike Mäder, Julia Bandow, Thomas Schweder
Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.
Microbiology (Reading, Engl.): 2002, 148(Pt 11);3441-55
[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] (P p)