Drm

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  • Description: phosphopentomutase

Gene name drm
Synonyms yqkN
Essential no
Product phosphopentomutase
Function utilization of deoxyribose
Metabolic function and regulation of this protein in SubtiPathways:
Nucleoside catabolism, Nucleotides (regulation)
MW, pI 43 kDa, 4.974
Gene length, protein length 1182 bp, 394 aa
Immediate neighbours pupG, ripX
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Drm context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Drm expression.png




























Categories containing this gene/protein

utilization of nucleotides, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU23500

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate (according to Swiss-Prot)
  • Protein family: phosphopentomutase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on (Thr-87 OR Thr-89) PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3M8W (from B. cereus, 77% identity, 86% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced in the presence of nucleosides (deoxyribose 5-phosphate and ribose 5-phosphate act as molecular inducers) PubMed
    • subject to repression by glucose PubMed
  • 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

Additional publications: PubMed

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

R Schuch, A Garibian, H H Saxild, P J Piggot, P Nygaard
Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon.
Microbiology (Reading): 1999, 145 ( Pt 10);2957-66
[PubMed:10537218] [WorldCat.org] [DOI] (P p)