Drm

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  • Description: phosphopentomutase

Gene name drm
Synonyms yqkN
Essential no
Product phosphopentomutase
Function utilization of deoxyribose
Gene expression levels in SubtiExpress: drm
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
Sequences Protein DNA DNA_with_flanks
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

CcpA regulon

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 carbon catabolite repression (CcpA) 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

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

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)