TrpE

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  • Description: anthranilate synthase (subunit I)

Gene name trpE
Synonyms
Essential no
Product anthranilate synthase (subunit I)
Function biosynthesis of tryptophan
Interactions involving this protein in SubtInteract: TrpE
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp
MW, pI 57 kDa, 5.246
Gene length, protein length 1545 bp, 515 aa
Immediate neighbours trpD, aroH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
TrpE 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: BSU22680

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: subject to feedback inhibtion by tryptophan PubMed

Database entries

  • Structure: 1I7Q (from Serratia marcescens, 42% identity, 62% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
    • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
  • Additional information:
    • subject to feedback inhibtion by tryptophan PubMed
    • 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

Reviews

The trpE RNA switch


Other original publications

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