YrhJ

• Description: similar to cytochrome P450 / NADPH-cytochrome P450 reductase
  
  

Gene name	yrhJ
Synonyms
Essential	no
Product	unknown
Function	unknown
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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU27160

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

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:

• UniProt: O08336

• KEGG entry: [3]

• E.C. number: 1.6.2.4

Expression and regulation

• Operon: fatR-yrhJ PubMed

• Sigma factor: SigM PubMed

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

• Regulatory mechanism:
  • FatR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)