Difference between revisions of "ThiD"

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(References)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=2I5B 2I5B] {{PubMed|16978644}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31620 O31620]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31620 O31620]
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<pubmed>19348578 </pubmed>
 
<pubmed>19348578 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>14973012,, </pubmed>
+
<pubmed>14973012,16978644 , </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:09, 3 February 2010

  • 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)
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



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:
  • Interactions:
  • Localization:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

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)