Difference between revisions of "CysK"

From SubtiWiki
Jump to: navigation, search
Line 84: Line 84:
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P37887 P37887]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P37887 P37887]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU00730]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU00730]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.5.1.47 2.5.1.47]  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.5.1.47 2.5.1.47]  

Revision as of 01:50, 25 June 2009

  • Description: trigger enzyme: cysteine synthetase A and control of CymR activity

Gene name cysK
Synonyms
Essential no
Product cysteine synthetase A
Function biosynthesis of cysteine, control of CymR activity
Metabolic function and regulation of this protein in SubtiPathways:
Cys, Met & Sulfate assimilation
MW, pI 32 kDa, 5.492
Gene length, protein length 924 bp, 308 aa
Immediate neighbours yacD, pabB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CysK context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU00730

Phenotypes of a mutant

constitutive expression of the cysH-cysP-sat-cysC-ylnD-ylnE-ylnF operon, auxotrophic for cysteine

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: O(3)-acetyl-L-serine + H2S = L-cysteine + acetate (according to Swiss-Prot)
  • Protein family: cysteine synthase/cystathionine beta-synthase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions: CymR-CysK, the complex is formed in the presence of cysteine, and results in DNA binding and repression of genes of cysteine biosynthesis PubMed
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: repressed by casamino acids PubMed, repressed in the presence of cysteine CymR
    • repressed in the presence of cysteine (CymR) PubMed
  • Regulatory mechanism: CymR: transcription repression
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Isabelle Martin-Verstraete, Institute Pasteur, Paris, France

Your additional remarks

References

Catherine Tanous, Olga Soutourina, Bertrand Raynal, Marie-Françoise Hullo, Peggy Mervelet, Anne-Marie Gilles, Philippe Noirot, Antoine Danchin, Patrick England, Isabelle Martin-Verstraete
The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis.
J Biol Chem: 2008, 283(51);35551-60
[PubMed:18974048] [WorldCat.org] [DOI] (P p)

Marie-Françoise Hullo, Sandrine Auger, Olga Soutourina, Octavian Barzu, Mireille Yvon, Antoine Danchin, Isabelle Martin-Verstraete
Conversion of methionine to cysteine in Bacillus subtilis and its regulation.
J Bacteriol: 2007, 189(1);187-97
[PubMed:17056751] [WorldCat.org] [DOI] (P p)

Sergine Even, Pierre Burguière, Sandrine Auger, Olga Soutourina, Antoine Danchin, Isabelle Martin-Verstraete
Global control of cysteine metabolism by CymR in Bacillus subtilis.
J Bacteriol: 2006, 188(6);2184-97
[PubMed:16513748] [WorldCat.org] [DOI] (P p)

Daniela Albanesi, Maria Cecilia Mansilla, Gustavo E Schujman, Diego de Mendoza
Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation.
J Bacteriol: 2005, 187(22);7631-8
[PubMed:16267287] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)