Difference between revisions of "BkdB"

From SubtiWiki
Jump to: navigation, search
Line 31: Line 31:
 
__TOC__
 
__TOC__
  
<br/><br/><br/><br/>
+
<br/><br/><br/><br/><br/><br/>
  
 
=The gene=
 
=The gene=

Revision as of 16:58, 22 June 2009

  • Description: 2-oxoisovalerate dehydrogenase (E2 subunit, lipoamide acyltransferase)

Gene name bkdB
Synonyms bfmBB, bfmB2, bkd
Essential no
Product 2-oxoisovalerate dehydrogenase
(E2 subunit, lipoamide acyltransferase)
Function utilization of branched-chain keto acids
Metabolic function and regulation of this protein in SubtiPathways:
Ile, Leu, Val
MW, pI 45 kDa, 5.301
Gene length, protein length 1272 bp, 424 aa
Immediate neighbours bmrR, bkdAB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
BkdB context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU24030

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine (according to Swiss-Prot)
  • Protein family: 2-oxoacid dehydrogenase 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: Nucleoid (Heterogeneous) 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)