Difference between revisions of "SdaAB"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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<pubmed>22383849 22686449</pubmed>
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<pubmed>22383849 22686449 24161940 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:14, 29 November 2013

  • Description: L-serine deaminase

Gene name sdaAB
Synonyms yloW, sdaA
Essential no
Product L-serine deaminase (beta chain)
Function serine utilization
Gene expression levels in SubtiExpress: sdaAB
Metabolic function and regulation of this protein in SubtiPathways:
Ala, Gly, Ser
MW, pI 23 kDa, 5.103
Gene length, protein length 660 bp, 220 aa
Immediate neighbours yloV, sdaAA
Sequences Protein DNA DNA_with_flanks
Genetic context
SdaAB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdaAB expression.png















Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15850

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-serine = pyruvate + NH3 (according to Swiss-Prot)
  • Protein family: ACT domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Sigma factor:
  • 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

Xiao Lan Xu, Gregory A Grant
Identification and characterization of two new types of bacterial L-serine dehydratases and assessment of the function of the ACT domain.
Arch Biochem Biophys: 2013, 540(1-2);62-9
[PubMed:24161940] [WorldCat.org] [DOI] (I p)

Shawei Chen, Xiao Lan Xu, Gregory A Grant
Allosteric activation and contrasting properties of L-serine dehydratase types 1 and 2.
Biochemistry: 2012, 51(26);5320-8
[PubMed:22686449] [WorldCat.org] [DOI] (I p)

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)