Difference between revisions of "TrpD"

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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P03947 P03947]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P03947 P03947]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU22670]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU22670]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.4.2.18 2.4.2.18]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.4.2.18 2.4.2.18]

Revision as of 05:06, 25 June 2009

  • Description: anthranilate phosphoribosyltransferase

Gene name trpD
Synonyms
Essential no
Product anthranilate phosphoribosyltransferase
Function biosynthesis of tryptophan
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp
MW, pI 35 kDa, 4.904
Gene length, protein length 1014 bp, 338 aa
Immediate neighbours trpC, trpE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
TrpD context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU22670

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate (according to Swiss-Prot)
  • Protein family: 2-oxoacid dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • 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:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255] [WorldCat.org] [DOI] (P 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)

H Shimotsu, M I Kuroda, C Yanofsky, D J Henner
Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon.
J Bacteriol: 1986, 166(2);461-71
[PubMed:2422155] [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)