Difference between revisions of "YcnD"

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=References=
 
=References=
  
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<pubmed>16229462,17407181,, </pubmed>
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 07:00, 14 June 2009

  • Description: NADPH-FMN oxidoreductase, delivers reduced FMN to enzymes that require the reduced cofactor for activity

Gene name ycnD
Synonyms
Essential no
Product NADPH-FMN oxidoreductase
Function delivery of FMN to enzymes
MW, pI 27 kDa, 5.081
Gene length, protein length 747 bp, 249 aa
Immediate neighbours ycnC, ycnE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YcnD context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU03860

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: flavin oxidoreductase frp family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • 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

Van Duy Nguyen, Carmen Wolf, Ulrike Mäder, Michael Lalk, Peter Langer, Ulrike Lindequist, Michael Hecker, Haike Antelmann
Transcriptome and proteome analyses in response to 2-methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems involved in the catabolism of aromatic compounds in Bacillus subtilis.
Proteomics: 2007, 7(9);1391-408
[PubMed:17407181] [WorldCat.org] [DOI] (P p)

Alexander Morokutti, Andrzej Lyskowski, Sonja Sollner, Eva Pointner, Teresa B Fitzpatrick, Christoph Kratky, Karl Gruber, Peter Macheroux
Structure and function of YcnD from Bacillus subtilis, a flavin-containing oxidoreductase.
Biochemistry: 2005, 44(42);13724-33
[PubMed:16229462] [WorldCat.org] [DOI] (P p)

  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed