Difference between revisions of "YlnE"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15620&redirect=T BSU15620]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cysHP-sat-cysC-ylnDEF.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/cysHP-sat-cysC-ylnDEF.html]
Line 96: Line 97:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15620&redirect=T BSU15620]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 13:41, 2 April 2014

  • Description: probable siroheme ferrochelatase

Gene name ylnE
Synonyms
Essential no
Product probable siroheme ferrochelatase
Function siroheme biosynthesis, sulfite reduction
Gene expression levels in SubtiExpress: ylnE
Metabolic function and regulation of this protein in SubtiPathways:
ylnE
MW, pI 28 kDa, 6.063
Gene length, protein length 783 bp, 261 aa
Immediate neighbours ylnD, ylnF
Sequences Protein DNA DNA_with_flanks
Genetic context
YlnE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YlnE expression.png




























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: BSU15620

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Siroheme + 2 H+ = sirohydrochlorin + Fe2+ (according to Swiss-Prot)
  • Protein family: SirB subfamily (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: [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)