Difference between revisions of "PdxK"

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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39610 P39610]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39610 P39610]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU38020]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU38020]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.4.7 2.7.4.7]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.4.7 2.7.4.7]

Revision as of 05:00, 25 June 2009

  • Description: pyridoxal kinase

Gene name thiD
Synonyms ywdB, ipa-52r, pdxK
Essential no
Product pyridoxal kinase
Function biosynthesis of pyridoxal phosphate
MW, pI 28 kDa, 4.922
Gene length, protein length 813 bp, 271 aa
Immediate neighbours ywdD, ywdA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThiD context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU38020

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine (according to Swiss-Prot)
  • Protein family: thiD family (according to Swiss-Prot)
  • Paralogous protein(s): YjbV

Extended information on the protein

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

Database entries

  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Joseph A Newman, Sanjan K Das, Svetlana E Sedelnikova, David W Rice
Cloning, purification and preliminary crystallographic analysis of a putative pyridoxal kinase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2006, 62(Pt 10);1006-9
[PubMed:17012797] [WorldCat.org] [DOI] (I p)

Joo-Heon Park, Kristin Burns, Cynthia Kinsland, Tadhg P Begley
Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase.
J Bacteriol: 2004, 186(5);1571-3
[PubMed:14973012] [WorldCat.org] [DOI] (P p)