Difference between revisions of "IlvD"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 3104 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 3104 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1545 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1545 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4271 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1398 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2083 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:09, 17 April 2014

  • Description: dihydroxy-acid dehydratase (2,3-dihydroxy-3-methylbutanoate, 2,3-dihydroxy-3-methylpentanoate)

Gene name ilvD
Synonyms
Essential no
Product dihydroxy-acid dehydratase
(2,3-dihydroxy-3-methylbutanoate,
2,3-dihydroxy-3-methylpentanoate)
Function biosynthesis of branched-chain amino acids
Gene expression levels in SubtiExpress: ilvD
Metabolic function and regulation of this protein in SubtiPathways:
ilvD
MW, pI 59 kDa, 5.315
Gene length, protein length 1674 bp, 558 aa
Immediate neighbours brxA, ypgR
Sequences Protein DNA DNA_with_flanks
Genetic context
IlvD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, most abundant proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

  • Locus tag: BSU21870

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 3104 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1545 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4271 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1398 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2083 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P 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)