Difference between revisions of "AroE"

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  <big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
 
  <big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
 
  [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
  [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
<pubmed>,3106153, </pubmed>
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<pubmed>3924737,3106153,6436812 1551827 8419914</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 20:20, 19 November 2011

  • Description: 3-phosphoshikimate 1-carboxyvinyltransferase

Gene name aroE
Synonyms
Essential no
Product 3-phosphoshikimate 1-carboxyvinyltransferase
Function biosynthesis of aromatic amino acids
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp
MW, pI 45 kDa, 6.341
Gene length, protein length 1284 bp, 428 aa
Immediate neighbours ypiA, tyrA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AroE context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

  • Locus tag: BSU22600

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate (according to Swiss-Prot)
  • Protein family: ABC transporter family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3RMT (from B. halodurans, 68% identity, 87% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
    • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

D J Henner, L Band, G Flaggs, E Chen
The organization and nucleotide sequence of the Bacillus subtilis hisH, tyrA and aroE genes.
Gene: 1986, 49(1);147-52
[PubMed:3106153] [WorldCat.org] [DOI] (P p)

D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737] [WorldCat.org] [DOI] (P p)

H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812] [WorldCat.org] [DOI] (P p)