Difference between revisions of "ThiD"

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* '''Description:''' 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase<br/><br/>
 
 
 
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Revision as of 10:10, 9 August 2012

  • Description: 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase

Gene name thiD
Synonyms yjbV
Essential no
Product 4-amino-5-hydroxymethyl-2-methylpyrimidine
pyrophosphate kinase
Function biosynthesis of thiamine pyrophosphate (TPP)
Gene expression levels in SubtiExpress: thiD
Metabolic function and regulation of this protein in SubtiPathways:
Thiamin
MW, pI 28 kDa, 5.709
Gene length, protein length 813 bp, 271 aa
Immediate neighbours thiF, fabI
Gene sequence (+200bp) Protein sequence
Genetic context
YjbV context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ThiD expression.png




























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

Thi-box

The gene

Basic information

  • Locus tag: BSU11710

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): PdxK

Extended information on the protein

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

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • 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

Reviews

Christopher T Jurgenson, Tadhg P Begley, Steven E Ealick
The structural and biochemical foundations of thiamin biosynthesis.
Annu Rev Biochem: 2009, 78;569-603
[PubMed:19348578] [WorldCat.org] [DOI] (I p)

T P Begley, D M Downs, S E Ealick, F W McLafferty, A P Van Loon, S Taylor, N Campobasso, H J Chiu, C Kinsland, J J Reddick, J Xi
Thiamin biosynthesis in prokaryotes.
Arch Microbiol: 1999, 171(5);293-300
[PubMed:10382260] [WorldCat.org] [DOI] (P p)


Original publications

Joseph A Newman, Sanjan K Das, Svetlana E Sedelnikova, David W Rice
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parallel emergence of enzyme activity during evolution.
J Mol Biol: 2006, 363(2);520-30
[PubMed:16978644] [WorldCat.org] [DOI] (P 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)