Difference between revisions of "TyrA"

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* '''Locus tag:''' BSU22610
 
* '''Locus tag:''' BSU22610
 
[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=tyrA_2369251_2370366_-1 Expression]
 
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 10:19, 28 January 2012

  • 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
TyrA 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: BSU22610

Phenotypes of a mutant

Database entries

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

Additional information

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

Database entries

  • Structure:
  • 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)

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)