BioI

• Description: cytochrome P450 enzyme
  
  

Gene name	bioI
Synonyms
Essential	no
Product	cytochrome P450 enzyme
Function	biosynthesis of biotin
MW, pI	44 kDa, 6.2
Gene length, protein length	1185 bp, 395 aa
Immediate neighbours	ytbQ, bioB
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: BSU30190

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: formation of pimelic acid via a multiple-step oxidative cleavage of long-chain fatty acids

• Protein family: cytochrome P450 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: Fer-BioI PubMed, YkuP-BioI PubMed, AcpA-BioI PubMed

• Localization:

Database entries

• Structure: 3EJE (complex with AcpA) PubMed

• UniProt: P53554

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: bioW-bioA-bioF-bioD-bioB-bioI-ytbQ PubMed

• Sigma factor:

• Regulation:
  • repressed in the presence of biotin (BirA) PubMed

• Regulatory mechanism:
  • BirA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Max J Cryle
Selectivity in a barren landscape: the P450(BioI)-ACP complex.
Biochem Soc Trans: 2010, 38(4);934-9
[PubMed:20658980] [WorldCat.org] [DOI] (I p)

Max J Cryle, Ilme Schlichting
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
Proc Natl Acad Sci U S A: 2008, 105(41);15696-701
[PubMed:18838690] [WorldCat.org] [DOI] (I p)

Rachel J Lawson, David Leys, Michael J Sutcliffe, Carol A Kemp, Myles R Cheesman, Susan J Smith, John Clarkson, W Ewen Smith, Ihtshamul Haq, John B Perkins, Andrew W Munro
Thermodynamic and biophysical characterization of cytochrome P450 BioI from Bacillus subtilis.
Biochemistry: 2004, 43(39);12410-26
[PubMed:15449931] [WorldCat.org] [DOI] (P p)

Rachel J Lawson, Claes von Wachenfeldt, Ihtshamul Haq, John Perkins, Andrew W Munro
Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: biophysical properties and interactions with cytochrome P450 BioI.
Biochemistry: 2004, 43(39);12390-409
[PubMed:15449930] [WorldCat.org] [DOI] (P p)

Amanda J Green, Andrew W Munro, Myles R Cheesman, Graeme A Reid, Claes von Wachenfeldt, Stephen K Chapman
Expression, purification and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI.
J Inorg Biochem: 2003, 93(1-2);92-9
[PubMed:12538057] [WorldCat.org] [DOI] (P p)

J E Stok, J De Voss
Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis.
Arch Biochem Biophys: 2000, 384(2);351-60
[PubMed:11368323] [WorldCat.org] [DOI] (P p)

J B Perkins, S Bower, C L Howitt, R R Yocum, J Pero
Identification and characterization of transcripts from the biotin biosynthetic operon of Bacillus subtilis.
J Bacteriol: 1996, 178(21);6361-5
[PubMed:8892842] [WorldCat.org] [DOI] (P p)

S Bower, J B Perkins, R R Yocum, C L Howitt, P Rahaim, J Pero
Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon.
J Bacteriol: 1996, 178(14);4122-30
[PubMed:8763940] [WorldCat.org] [DOI] (P p)