yetO
168
cytochrome P450 (CYP102A2)/ NADPH-cytochrome P450 reductase
Locus
BSU_07250
Molecular weight
119.26 kDa
Isoelectric point
5.73
Function
fatty acid metabolism
Product
NADPH-cytochrome P450 reductase
Essential
no
E.C.
1.6.2.4
Synonyms
yetO, yfnJ
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG2124 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
792,682 795,867
The protein
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
alkane + O2 + reduced [NADPH—hemoprotein reductase] --> primary alcohol + H+ + H2O + oxidized [NADPH—hemoprotein reductase] (according to UniProt)
NADPH + 2 oxidized [cytochrome P450] --> H+ + NADP+ + 2 reduced [cytochrome P450] (according to UniProt)
Protein family
cytochrome P450 family (according to UniProt)
Flavodoxin-like domain (aa 493-632) (according to UniProt)
FAD-binding FR-type domain (aa 671-904) (according to UniProt)
FAD (according to UniProt)
Structure
2X7Y (PDB) (from Bacillus megaterium; 66% identity, 87% similarity) PubMed
Paralogous protein(s)
cytoplasm (according to Swiss-Prot)
Expression and Regulation
Operons
Biological materials
Mutant
MGNA-C225 (yfnJ::erm), available at the NBRP B. subtilis, Japan
References
Enzyme-controlled nitrogen-atom transfer enables regiodivergent C-H amination.
Journal of the American Chemical Society. 2014 Nov 05; 136(44):15505-8. doi:10.1021/ja509308v. PMID:25325618
The role of active-site Phe87 in modulating the organic co-solvent tolerance of cytochrome P450 BM3 monooxygenase.
Acta crystallographica. Section F, Structural biology and crystallization communications. 2012 Sep 01; 68(Pt 9):1013-7. doi:10.1107/S1744309112031570. PMID:22949185
Cytochrome P450 102A2 Catalyzes Efficient Oxidation of Sodium Dodecyl Sulphate: A Molecular Tool for Remediation.
Enzyme research. 2010 Jul 01; 2010:125429. doi:10.4061/2010/125429. PMID:21048857
Preparative use of isolated CYP102 monooxygenases -- a critical appraisal.
Journal of biotechnology. 2006 Aug 05; 124(4):662-9. . PMID:16716428
Engineering the substrate specificity of cytochrome P450 CYP102A2 by directed evolution: production of an efficient enzyme for bioconversion of fine chemicals.
Biomolecular engineering. 2005 Jun; 22(1-3):81-8. . PMID:15857787
Cloning, expression and characterisation of CYP102A2, a self-sufficient P450 monooxygenase from Bacillus subtilis.
Applied microbiology and biotechnology. 2004 Dec; 66(2):180-6. . PMID:15375636
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Biochemistry. 2004 May 11; 43(18):5474-87. . PMID:15122913
Fatty-acid-displaced transcriptional repressor, a conserved regulator of cytochrome P450 102 transcription in Bacillus species.
Archives of microbiology. 2001 Dec; 176(6):459-64. . PMID:11734890
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Time of last update: 2025-04-10 01:28:22
Author of last update: Melvin.boenninger