Difference between revisions of "AroA"

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* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
* '''Effectors of protein activity:'''
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* '''Effectors of protein activity:''' subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed]
  
 
* '''Interactions:'''
 
* '''Interactions:'''
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
* '''Additional information:'''  
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* '''Additional information:''' subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed]
  
 
=Biological materials =
 
=Biological materials =

Revision as of 05:41, 28 May 2009

  • Description: 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase / chorismate mutase-isozyme 3

Gene name aroA
Synonyms aroG
Essential no
Product 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase /

chorismate mutase-isozyme 3

Function biosynthesis of aromatic amino acids
MW, pI 39 kDa, 5.341
Gene length, protein length 1074 bp, 358 aa
Immediate neighbours ccpA, ytxJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AroA context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate (according to Swiss-Prot)
  • Protein family: class-I DAHP synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-2 PubMed, phosphorylation on Thr-4 PubMed
  • Cofactor(s):
  • Effectors of protein activity: subject to feedback inhibition PubMed
  • Interactions:
  • Localization:

Database entries

  • Structure:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to feedback inhibition PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

  1. Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
  2. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed