TyrA

• Description: prephenate dehydrogenase
  
  

Gene name	tyrA
Synonyms
Essential	no
Product	prephenate dehydrogenase
Function	biosynthesis of tyrosine
Gene expression levels in SubtiExpress: tyrA
Metabolic function and regulation of this protein in SubtiPathways: tyrA
MW, pI	41 kDa, 5.471
Gene length, protein length	1113 bp, 371 aa
Immediate neighbours	aroE, hisC
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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)

• Expression browser: tyrA PubMed

• 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

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

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)

E W Nester, R A Jensen
Control of aromatic acid biosynthesis in Bacillus subtilis: sequenial feedback inhibition.
J Bacteriol: 1966, 91(4);1594-8
[PubMed:4956345] [WorldCat.org] [DOI] (P p)