Difference between revisions of "YkuN"

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* '''Modification:'''
 
* '''Modification:'''
  
* '''[[Cofactors]]:''' FMN
+
* '''[[Cofactors]]:''' FMN {{PubMed|25194416}}
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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** [[YjiB]]-[[YkuN]] {{PubMed|20186410}}
 
** [[YjiB]]-[[YkuN]] {{PubMed|20186410}}
 
** [[Des]]-[[YkuN]] (electron transfer to [[Des]]) {{PubMed|21665975}}
 
** [[Des]]-[[YkuN]] (electron transfer to [[Des]]) {{PubMed|21665975}}
 +
** [[YumC]]-[[YkuN]] (electron transfer from NADPH via [[YumC]] to [[YkuN]]) {{PubMed|25194416}}
 +
** [[Nos]]-[[YkuN]] (electron transfer from to [[Nos]]) {{PubMed|25194416}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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=References=
 
=References=
<pubmed>15449930,17127770 ,12354229, 20186410 24214949 21665975</pubmed>
+
<pubmed>15449930,17127770 ,12354229, 20186410 24214949 21665975 25194416 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:34, 19 September 2014

  • Description: flavodoxin, binds FMN, replaces ferredoxin under conditions of iron limitation, probably involved in electron transfer to nitric oxide synthase

Gene name ykuN
Synonyms
Essential no
Product flavodoxin
Function electron transfer
Gene expression levels in SubtiExpress: ykuN
Interactions involving this protein in SubtInteract: YkuN
Metabolic function and regulation of this protein in SubtiPathways:
ykuN
MW, pI 17 kDa, 3.827
Gene length, protein length 474 bp, 158 aa
Immediate neighbours ccpC, ykuO
Sequences Protein DNA DNA_with_flanks
Genetic context
YkuN context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YkuN expression.png















Categories containing this gene/protein

electron transport/ other

This gene is a member of the following regulons

Fur regulon, NsrR regulon, ResD regulon

The gene

Basic information

  • Locus tag: BSU14150

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: flavodoxin-like domain (according to Swiss-Prot)
  • Paralogous protein(s): YkuP

Extended information on the protein

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

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • induced upon iron starvation (Fur) PubMed
    • expressed under anaerobic conditions (ResD) PubMed
    • induced by nitric oxide under anaerobic conditions (NsrR) PubMed
  • 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

Jeffrey K Holden, Nathan Lim, Thomas L Poulos
Identification of redox partners and development of a novel chimeric bacterial nitric oxide synthase for structure activity analyses.
J Biol Chem: 2014, 289(42);29437-45
[PubMed:25194416] [WorldCat.org] [DOI] (I p)

Bernadette Henares, Sushma Kommineni, Onuma Chumsakul, Naotake Ogasawara, Shu Ishikawa, Michiko M Nakano
The ResD response regulator, through functional interaction with NsrR and fur, plays three distinct roles in Bacillus subtilis transcriptional control.
J Bacteriol: 2014, 196(2);493-503
[PubMed:24214949] [WorldCat.org] [DOI] (I p)

Lorena Chazarreta-Cifre, Leticia Martiarena, Diego de Mendoza, Silvia G Altabe
Role of ferredoxin and flavodoxins in Bacillus subtilis fatty acid desaturation.
J Bacteriol: 2011, 193(16);4043-8
[PubMed:21665975] [WorldCat.org] [DOI] (I p)

Marco Girhard, Tobias Klaus, Yogan Khatri, Rita Bernhardt, Vlada B Urlacher
Characterization of the versatile monooxygenase CYP109B1 from Bacillus subtilis.
Appl Microbiol Biotechnol: 2010, 87(2);595-607
[PubMed:20186410] [WorldCat.org] [DOI] (I p)

Zhi-Qiang Wang, Rachel J Lawson, Madhavan R Buddha, Chin-Chuan Wei, Brian R Crane, Andrew W Munro, Dennis J Stuehr
Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.
J Biol Chem: 2007, 282(4);2196-202
[PubMed:17127770] [WorldCat.org] [DOI] (P p)

Rachel J Lawson, Claes von Wachenfeldt, Ihtshamul Haq, John Perkins, Andrew W Munro
Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI.
Biochemistry: 2004, 43(39);12390-409
[PubMed:15449930] [WorldCat.org] [DOI] (P p)

Noel Baichoo, Tao Wang, Rick Ye, John D Helmann
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.
Mol Microbiol: 2002, 45(6);1613-29
[PubMed:12354229] [WorldCat.org] [DOI] (P p)