Difference between revisions of "AroA"

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(Expression and regulation)
(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1VR6 1VR6] (from ''Thermotoga maritima'', 51% identity, 68% similarity)
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39912 P39912]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39912 P39912]

Revision as of 10:55, 19 February 2010

  • 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
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp
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

  • Locus tag: BSU29750

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: 1VR6 (from Thermotoga maritima, 51% identity, 68% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

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)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221] [WorldCat.org] [DOI] (P p)