Difference between revisions of "PdxK"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38020&redirect=T BSU38020]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/thiD.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/thiD.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU38020&redirect=T BSU38020]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2IB5 2IB5]
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2IB5 2IB5]

Revision as of 15:07, 2 April 2014

  • Description: pyridoxine, pyridoxal, and pyridoxamine kinase

Gene name pdxK
Synonyms ywdB, ipa-52r, thiD
Essential no
Product pyridoxine, pyridoxal, and pyridoxamine kinase
Function biosynthesis of pyridoxal phosphate
Gene expression levels in SubtiExpress: pdxK
MW, pI 28 kDa, 4.922
Gene length, protein length 813 bp, 271 aa
Immediate neighbours ywzG, ywdA
Sequences Protein DNA DNA_with_flanks
Genetic context
ThiD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PdxK expression.png
























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

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): ThiD

Extended information on the protein

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

Database entries

  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Sigma factor:
  • 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)

A Fouet, A Klier, G Rapoport
Nucleotide sequence of the sucrase gene of Bacillus subtilis.
Gene: 1986, 45(2);221-5
[PubMed:3100393] [WorldCat.org] [DOI] (P p)