Difference between revisions of "IlvA"

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(Biological materials)
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}
 
=The protein=
 
=The protein=
  

Revision as of 17:23, 30 November 2010

  • Description: threonine dehydratase

Gene name ilvA
Synonyms
Essential no
Product threonine dehydratase
Function biosynthesis of branched-chain amino acids
Metabolic function and regulation of this protein in SubtiPathways:
Ile, Leu, Val
MW, pI 46 kDa, 5.538
Gene length, protein length 1266 bp, 422 aa
Immediate neighbours ypmP, yplP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
IlvA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU21770

Phenotypes of a mutant

Database entries

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

Additional information

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-threonine = 2-oxobutanoate + NH3 (according to Swiss-Prot)
  • Protein family: ccmF/cycK/ccl1/nrfE/ccsA 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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion: pGP519 (in pAC5), available in Stülke lab
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Boris R Belitsky, Abraham L Sonenshein
Genetic and biochemical analysis of CodY-binding sites in Bacillus subtilis.
J Bacteriol: 2008, 190(4);1224-36
[PubMed:18083814] [WorldCat.org] [DOI] (I p)

Ulrike Mäder, Susanne Hennig, Michael Hecker, Georg Homuth
Transcriptional organization and posttranscriptional regulation of the Bacillus subtilis branched-chain amino acid biosynthesis genes.
J Bacteriol: 2004, 186(8);2240-52
[PubMed:15060025] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)