Difference between revisions of "DeoD"

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<pubmed> 21424839 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:12, 23 March 2011

  • Description: purine nucleoside phosphorylase

Gene name deoD
Synonyms
Essential no
Product purine nucleoside phosphorylase
Function purine salvage and interconversion
Metabolic function and regulation of this protein in SubtiPathways:
Purine salvage, Nucleoside catabolism
MW, pI 25 kDa, 4.978
Gene length, protein length 699 bp, 233 aa
Immediate neighbours yodJ, yodL
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DeoD context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU19630

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: membrane (according to Swiss-Prot)

Database entries

  • Structure: 1XE3 (from Bacillus anthracis, 71% identity, 85% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • 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

Haojian Li, Guoqiang Zhang, Aihua Deng, Ning Chen, Tingyi Wen
De novo engineering and metabolic flux analysis of inosine biosynthesis in Bacillus subtilis.
Biotechnol Lett: 2011, 33(8);1575-80
[PubMed:21424839] [WorldCat.org] [DOI] (I p)