Difference between revisions of "Drm"

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(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2I09 2I09] (from ''Streptococcus mutans'', 56% identity, 71% similarity)
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3M8W 3M8W] (from ''B. cereus'', 77% identity, 86% similarity)
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P46353 P46353]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P46353 P46353]

Revision as of 16:41, 10 January 2011

  • 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







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, PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure: 3M8W (from B. cereus, 77% identity, 86% similarity)
  • 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

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)