Drm

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:

Database entries

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

• UniProt: P46353

• KEGG entry: [3]

• E.C. number: 5.4.2.7

Expression and regulation

• Operon: drm-pupG PubMed

• Expression browser: drm PubMed

• Sigma factor: SigA PubMed

• 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:
  • CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)