TyrA

• Description: prephenate dehydrogenase
  
  

Gene name	tyrA
Synonyms
Essential	no
Product	prephenate dehydrogenase
Function	biosynthesis of tyrosine
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp
MW, pI	41 kDa, 5.471
Gene length, protein length	1113 bp, 371 aa
Immediate neighbours	aroE, hisC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context 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: BSU22610

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Prephenate + NAD⁺ = 4-hydroxyphenylpyruvate + CO₂ + NADH (according to Swiss-Prot)

• Protein family: HisMQ subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: subject to feedback inhibtion by tyrosine PubMed

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P20692

• KEGG entry: [3]

• E.C. number: 1.3.1.12

Expression and regulation

• Operon:
  • aroF-aroB-aroH-trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE (according to DBTBS)
  • trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE PubMed
  • hisC-tyrA-aroE (according to DBTBS)

• Sigma factor:
  • trpE: SigA PubMed

• Regulation:
  • induction by tryptophan (TRAP) PubMed

• 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:

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