BkdAA

From SubtiWiki
Revision as of 11:10, 7 January 2014 by 134.76.70.252 (talk)
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
Gene expression levels in SubtiExpress: bkdAA
Metabolic function and regulation of this protein in SubtiPathways:
bkdAA
MW, pI 36 kDa, 4.778
Gene length, protein length 990 bp, 330 aa
Immediate neighbours bkdAB, lpdV
Sequences Protein DNA DNA_with_flanks
Genetic context
BkdAA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BkdAA expression.png















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

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)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1UMB (from Thermus thermophilus, 42% identity, 57% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

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

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)