Difference between revisions of "YrhJ"

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(Basic information/ Evolution)
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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
** hydroxylates medium-chain fatty acids in subterminal positions
+
** hydroxylates medium-chain fatty acids in subterminal positions {{PubMed|14741768}}
  
 
* '''Protein family:'''
 
* '''Protein family:'''

Revision as of 13:10, 11 August 2010

Gene name yrhJ
Synonyms
Essential no
Product NADPH-cytochrome P450 reductase
Function fatty acid metabolism
MW, pI 118 kDa, 6.017
Gene length, protein length 3162 bp, 1054 aa
Immediate neighbours yrhK, fatR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YrhJ context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU27160

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • hydroxylates medium-chain fatty acids in subterminal positions PubMed
  • Protein family:
  • Paralogous protein(s): YetO

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced by unsaturated fatty acids (FatR) 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

Mattias C U Gustafsson, Olivier Roitel, Ker R Marshall, Michael A Noble, Stephen K Chapman, Antonio Pessegueiro, Armand J Fulco, Myles R Cheesman, Claes von Wachenfeldt, Andrew W Munro
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Biochemistry: 2004, 43(18);5474-87
[PubMed:15122913] [WorldCat.org] [DOI] (P p)

Oliver Lentz, Vlada Urlacher, Rolf D Schmid
Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis.
J Biotechnol: 2004, 108(1);41-9
[PubMed:14741768] [WorldCat.org] [DOI] (P p)

Penny D Thackray, Anne Moir
SigM, an extracytoplasmic function sigma factor of Bacillus subtilis, is activated in response to cell wall antibiotics, ethanol, heat, acid, and superoxide stress.
J Bacteriol: 2003, 185(12);3491-8
[PubMed:12775685] [WorldCat.org] [DOI] (P p)

M C Gustafsson, C N Palmer, C R Wolf, C von Wachenfeldt
Fatty-acid-displaced transcriptional repressor, a conserved regulator of cytochrome P450 102 transcription in Bacillus species.
Arch Microbiol: 2001, 176(6);459-64
[PubMed:11734890] [WorldCat.org] [DOI] (P p)

T R Lee, H P Hsu, G C Shaw
Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3 operon by the BscR repressor and differential induction of cytochrome CYP102A3 expression by oleic acid and palmitate.
J Biochem: 2001, 130(4);569-74
[PubMed:11574077] [WorldCat.org] [DOI] (P p)

C N Palmer, M C Gustafsson, H Dobson, C von Wachenfeldt, C R Wolf
Adaptive responses to fatty acids are mediated by the regulated expression of cytochromes P450.
Biochem Soc Trans: 1999, 27(4);374-8
[PubMed:10917605] [WorldCat.org] [DOI] (P p)