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
Metabolic function and regulation of this protein in SubtiPathways: YetO
MW, pI	119 kDa, 5.732
Gene length, protein length	3183 bp, 1061 aa
Immediate neighbours	yetN, yfnI
Sequences	Protein DNA DNA_with_flanks
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

• BsubCyc: BSU07250

• 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

• BsubCyc: BSU07250

• 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)