Difference between revisions of "YrhJ"
(→Basic information/ Evolution) |
|||
Line 6: | Line 6: | ||
|''yrhJ'' | |''yrhJ'' | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''cypE '' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no |
Revision as of 13:11, 11 August 2010
- Description: similar to cytochrome P450 / 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
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:
- UniProt: O08336
- KEGG entry: [3]
- E.C. number: 1.6.2.4
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
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)