Difference between revisions of "YetO"
(→Basic information/ Evolution) |
|||
| Line 57: | Line 57: | ||
* '''Protein family:''' | * '''Protein family:''' | ||
| − | * '''Paralogous protein(s):''' | + | * '''Paralogous protein(s):''' [[YrhJ]] |
=== Extended information on the protein === | === Extended information on the protein === | ||
Revision as of 13:09, 11 August 2010
- Description: cytochrome P450 / NADPH-cytochrome P450 reductase
| Gene name | yetO |
| Synonyms | yfnJ , cypD |
| Essential | no |
| Product | NADPH-cytochrome P450 reductase |
| Function | fatty acid metabolism |
| MW, pI | 119 kDa, 5.732 |
| Gene length, protein length | 3183 bp, 1061 aa |
| Immediate neighbours | yetN, yfnI |
| 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: BSU07250
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
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
- Structure:
- UniProt: O08394
- KEGG entry: [2]
- E.C. number: 1.6.2.4
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- 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
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)
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)
