Difference between revisions of "RhaM"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
{{SubtiWiki category|[[proteins of unknown function]]}}
+
{{SubtiWiki category|[[utilization of specific carbon sources]]}}
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:'''
+
* '''[[SubtInteract|Interactions]]:'''  
  
* '''Localization:''' cytoplasm (according to Swiss-Prot)
+
* '''[[Localization]]:'''
 +
** cytoplasm (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Operon:'''  
 
* '''Operon:'''  
 +
** ''[[rhaEW]]-[[rhaR]]-[[rhaB]]-[[rhaM]]-[[rhaA]]'' {{PubMed|22383849}}
 +
** ''[[rhaR]]-[[rhaB]]-[[rhaM]]-[[rhaA]]'' {{PubMed|22383849}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yulD_3199233_3199547_-1 yulD] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yulD_3199233_3199547_-1 yulD] {{PubMed|22383849}}
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=References=
 
=References=
<pubmed>24391637 </pubmed>
+
<pubmed>24391637 22383849</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:06, 7 June 2014

  • Description: mutarotase involved in rhamnose utilization

Gene name yulD
Synonyms
Essential no
Product mutarotase
Function utilization of rhamnose
Gene expression levels in SubtiExpress: yulD
MW, pI 12 kDa, 5.184
Gene length, protein length 312 bp, 104 aa
Immediate neighbours yulE, yulC
Sequences Protein DNA DNA_with_flanks
Genetic context
YulD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YulD expression.png















Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU31190

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Alpha-L-rhamnose = beta-L-rhamnose (according to Swiss-Prot)
  • Protein family: rhamnose mutarotase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • 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

Irina A Rodionova, Xiaoqing Li, Vera Thiel, Sergey Stolyar, Krista Stanton, James K Fredrickson, Donald A Bryant, Andrei L Osterman, Aaron A Best, Dmitry A Rodionov
Comparative genomics and functional analysis of rhamnose catabolic pathways and regulons in bacteria.
Front Microbiol: 2013, 4;407
[PubMed:24391637] [WorldCat.org] [DOI] (P e)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)