YetO

• Description: cytochrome P450 (CYP102A2)/ NADPH-cytochrome P450 reductase
  
  

Gene name	yetO
Synonyms	yfnJ , cypD
Essential	no
Product	NADPH-cytochrome P450 reductase
Function	fatty acid metabolism
Gene expression levels in SubtiExpress: yetO
MW, pI	119 kDa, 5.732
Gene length, protein length	3183 bp, 1061 aa
Immediate neighbours	yetN, yfnI
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

electron transport/ other, lipid metabolism/ other

The gene

Basic information

• Locus tag: BSU07250

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • oxidation of even- and odd-chain saturated and unsaturated fatty acids to the respective omega-3, omega-2 and omega-1 hydroxylated fatty acids PubMed

• Protein family:

• Paralogous protein(s): YrhJ

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2X7Y (from Bacillus megaterium; 66% identity, 87% similarity)

• UniProt: O08394

• KEGG entry: [2]

• E.C. number: 1.6.2.4

Expression and regulation

• Operon:

• Expression browser: yetO PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Irene Axarli, Ariadne Prigipaki, Nikolaos E Labrou
Cytochrome P450 102A2 Catalyzes Efficient Oxidation of Sodium Dodecyl Sulphate: A Molecular Tool for Remediation.
Enzyme Res: 2010, 2010;125429
[PubMed:21048857] [WorldCat.org] [DOI] (I e)

Sabine Eiben, Leonard Kaysser, Steffen Maurer, Katja Kühnel, Vlada B Urlacher, Rolf D Schmid
Preparative use of isolated CYP102 monooxygenases -- a critical appraisal.
J Biotechnol: 2006, 124(4);662-9
[PubMed:16716428] [WorldCat.org] [DOI] (P p)

Irene Axarli, Ariadne Prigipaki, Nikolaos E Labrou
Engineering the substrate specificity of cytochrome P450 CYP102A2 by directed evolution: production of an efficient enzyme for bioconversion of fine chemicals.
Biomol Eng: 2005, 22(1-3);81-8
[PubMed:15857787] [WorldCat.org] [DOI] (P p)

M Budde, S C Maurer, R D Schmid, V B Urlacher
Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis.
Appl Microbiol Biotechnol: 2004, 66(2);180-6
[PubMed:15375636] [WorldCat.org] [DOI] (P p)

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)

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)