Difference between revisions of "Hom"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 2167 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 2167 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1723 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1723 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3436 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2047 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3239 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:08, 17 April 2014

  • Description: homoserine dehydrogenase (NADPH)

Gene name hom
Synonyms
Essential no
Product homoserine dehydrogenase (NADPH)
Function biosynthesis of methionine and threonine
Gene expression levels in SubtiExpress: hom
Metabolic function and regulation of this protein in SubtiPathways:
hom
MW, pI 47 kDa, 4.9
Gene length, protein length 1299 bp, 433 aa
Immediate neighbours thrC, yutH
Sequences Protein DNA DNA_with_flanks
Genetic context
Hom context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Hom expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, membrane proteins, most abundant proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

  • Locus tag: BSU32260

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H (according to Swiss-Prot)
  • Protein family: homoserine dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity: subject to feedback inhibition PubMed

Database entries

  • Structure: 2EJW (from Thermus thermophilus hb8, 37% identity, 57% similarity)
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:
  • Additional information:
    • subject to feedback inhibition PubMed
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2167 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1723 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3436 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2047 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3239 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • 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)

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [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, 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)

C Parsot, G N Cohen
Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II.
J Biol Chem: 1988, 263(29);14654-60
[PubMed:3139660] [WorldCat.org] (P p)