Difference between revisions of "YrhJ"
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** A [[ncRNA]] is predicted between ''[[yrhK]]'' and ''[[yrhJ]]'' {{PubMed|20525796}} | ||
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− | <pubmed>11734890,10917605 ,11574077,14741768,15122913, 12775685 16716428 16381045 </pubmed> | + | <pubmed>11734890,10917605 ,11574077,14741768,15122913, 12775685 16716428 16381045 20525796</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:23, 4 May 2011
- Description: cytochrome P450 (CYP102A3)/ NADPH-cytochrome P450 reductase
Gene name | yrhJ |
Synonyms | cypE |
Essential | no |
Product | NADPH-cytochrome P450 reductase |
Function | fatty acid metabolism |
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
|
Contents
Categories containing this gene/protein
electron transport/ other, lipid metabolism/ other, cell envelope stress proteins (controlled by SigM, W, X, Y), membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27160
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- hydroxylates medium-chain fatty acids in subterminal positions PubMed
- Protein family:
- Paralogous protein(s): YetO
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: 2X7Y (from Bacillus megaterium; 67% identity, 88% similarity)
- UniProt: O08336
- KEGG entry: [3]
- E.C. number: 1.6.2.4
Additional information
Expression and regulation
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796]
[WorldCat.org]
[DOI]
(I p)
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)
Oliver Lentz, Anton Feenstra, Tilo Habicher, Bernhard Hauer, Rolf D Schmid, Vlada B Urlacher
Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system.
Chembiochem: 2006, 7(2);345-50
[PubMed:16381045]
[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)
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)