Difference between revisions of "YlnD"

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m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
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* '''Operon:''' ''[[cysH]]-[[cysP]]-[[sat]]-[[cysC]]-[[ylnD]]-[[ylnE]]-[[ylnF]]'' {{PubMed|11004190}}
 
* '''Operon:''' ''[[cysH]]-[[cysP]]-[[sat]]-[[cysC]]-[[ylnD]]-[[ylnE]]-[[ylnF]]'' {{PubMed|11004190}}
  
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|11004190}}
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sumT_1634061_1634834_1 ylnD] {{PubMed|22383849}}
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* '''Sigma factor:''' [[SigA]] {{PubMed|11004190}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  

Revision as of 08:40, 13 April 2012

  • Description: probable uroporphyrin-III C-methyltransferase

Gene name ylnD
Synonyms
Essential no
Product probable uroporphyrin-III C-methyltransferase
Function siroheme biosynthesis , sulfite reduction
Metabolic function and regulation of this protein in SubtiPathways:
Cys, Met & Sulfate assimilation
MW, pI 28 kDa, 5.752
Gene length, protein length 771 bp, 257 aa
Immediate neighbours cysC, ylnE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YlnD context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

CymR regulon, S-box

The gene

Basic information

  • Locus tag: BSU15610

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
    • repressed in the presence of cysteine (CymR)
    • induced by methionine starvation (S-box) PubMed
  • Regulatory mechanism:
    • S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
    • CymR: transcription repression
  • 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

Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762] [WorldCat.org] [DOI] (I 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)

M C Mansilla, D Albanesi, D de Mendoza
Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis.
J Bacteriol: 2000, 182(20);5885-92
[PubMed:11004190] [WorldCat.org] [DOI] (P p)

Per Johansson, Lars Hederstedt
Organization of genes for tetrapyrrole biosynthesis in gram--positive bacteria.
Microbiology (Reading): 1999, 145 ( Pt 3);529-538
[PubMed:10217486] [WorldCat.org] [DOI] (P p)