Difference between revisions of "Drm"
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= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | + | {{SubtiWiki regulon|[[CcpA regulon]]}} | |
=The gene= | =The gene= | ||
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* '''Regulation:''' | * '''Regulation:''' | ||
** induced in the presence of nucleosides (deoxyribose 5-phosphate and ribose 5-phosphate act as molecular inducers) {{PubMed|10537218}} | ** induced in the presence of nucleosides (deoxyribose 5-phosphate and ribose 5-phosphate act as molecular inducers) {{PubMed|10537218}} | ||
| − | ** subject to repression | + | ** subject to carbon catabolite repression ([[CcpA]]) {{PubMed|22900538,10537218}} |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[CcpA]]: transcription repression {{PubMed|22900538}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
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=References= | =References= | ||
'''Additional publications:''' {{PubMed|21193409}} | '''Additional publications:''' {{PubMed|21193409}} | ||
| − | <pubmed> 10537218 17218307,17726680</pubmed> | + | <pubmed> 10537218 17218307,17726680 22900538</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:31, 21 August 2012
- 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 |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
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
- UniProt: P46353
- KEGG entry: [3]
- E.C. number: 5.4.2.7
Additional information
Expression and regulation
- Regulation:
- 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)
