Difference between revisions of "AsnH"

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(Expression and regulation)
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* '''[[Sigma factor]]:'''  
 
* '''[[Sigma factor]]:'''  
  
* '''Regulation:''' repressed by [[CodY]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
+
* '''Regulation:'''  
 
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
 
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
 
** repressed during logrithmic growth ([[AbrB]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15101989 PubMed]
 
** repressed during logrithmic growth ([[AbrB]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15101989 PubMed]
  
* '''Regulatory mechanism:''' [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed] 
+
* '''Regulatory mechanism:'''  
 
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
 
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
 
** [[AbrB]]:  transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15101989 PubMed]
 
** [[AbrB]]:  transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15101989 PubMed]

Revision as of 20:42, 10 February 2010

  • Description: asparagine synthase (glutamine-hydrolysing)

Gene name asnH
Synonyms yxaN
Essential no
Product asparagine synthase (glutamine-hydrolysing))
Function biosynthesis of asparagine
Metabolic function and regulation of this protein in SubtiPathways:
Asp, Asn
MW, pI 85 kDa, 5.528
Gene length, protein length 2241 bp, 747 aa
Immediate neighbours yxnB, yxaM
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AsnH context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU39920

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate (according to Swiss-Prot)
  • Protein family: asparagine synthetase 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

Expression and regulation

  • Regulation:
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
    • repressed during logrithmic growth (AbrB) 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

Mélanie A Hamon, Nicola R Stanley, Robert A Britton, Alan D Grossman, Beth A Lazazzera
Identification of AbrB-regulated genes involved in biofilm formation by Bacillus subtilis.
Mol Microbiol: 2004, 52(3);847-60
[PubMed:15101989] [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)

Ken-Ichi Yoshida, Izumi Ishio, Eishi Nagakawa, Yoshiyuki Yamamoto, Mami Yamamoto, Yasutaro Fujita
Systematic study of gene expression and transcription organization in the gntZ-ywaA region of the Bacillus subtilis genome.
Microbiology (Reading): 2000, 146 ( Pt 3);573-579
[PubMed:10746760] [WorldCat.org] [DOI] (P p)

K Yoshida, Y Fujita, S D Ehrlich
Three asparagine synthetase genes of Bacillus subtilis.
J Bacteriol: 1999, 181(19);6081-91
[PubMed:10498721] [WorldCat.org] [DOI] (P p)