Difference between revisions of "YjiB"
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− | * '''Description:''' | + | * '''Description:''' monooxygenase CYP109B1 <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || monooxygenase CYP109B1 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || oxidation of fatty acids |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 44 kDa, 5.379 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 44 kDa, 5.379 | ||
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' oxidation of saturated fatty acids (conversion up to 99%) and their methyl and ethyl esters (conversion up to 80%) at subterminal positions with a preference for the carbon atoms C11 and C12 counted from the carboxyl group {{PubMed|20186410}} |
* '''Protein family:''' cytochrome P450 family (according to Swiss-Prot) | * '''Protein family:''' cytochrome P450 family (according to Swiss-Prot) | ||
Line 70: | Line 70: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''Interactions:''' [[YjiB]]-[[YkuN]] {{PubMed|20186410}}, [[YjiB]]-[[YkuP]] {{PubMed|20186410}} |
* '''Localization:''' | * '''Localization:''' | ||
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=References= | =References= | ||
− | + | <pubmed>19591681 20186410 </pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:22, 27 February 2010
- Description: monooxygenase CYP109B1
Gene name | yjiB |
Synonyms | |
Essential | no |
Product | monooxygenase CYP109B1 |
Function | oxidation of fatty acids |
MW, pI | 44 kDa, 5.379 |
Gene length, protein length | 1188 bp, 396 aa |
Immediate neighbours | yjiA, yjiC |
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: BSU12210
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 saturated fatty acids (conversion up to 99%) and their methyl and ethyl esters (conversion up to 80%) at subterminal positions with a preference for the carbon atoms C11 and C12 counted from the carboxyl group PubMed
- 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:
- Localization:
Database entries
- Structure:
- UniProt: O34374
- KEGG entry: [2]
- E.C. number:
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
Marco Girhard, Tobias Klaus, Yogan Khatri, Rita Bernhardt, Vlada B Urlacher
Characterization of the versatile monooxygenase CYP109B1 from Bacillus subtilis.
Appl Microbiol Biotechnol: 2010, 87(2);595-607
[PubMed:20186410]
[WorldCat.org]
[DOI]
(I p)
Marco Girhard, Kazuhiro Machida, Masashi Itoh, Rolf D Schmid, Akira Arisawa, Vlada B Urlacher
Regioselective biooxidation of (+)-valencene by recombinant E. coli expressing CYP109B1 from Bacillus subtilis in a two-liquid-phase system.
Microb Cell Fact: 2009, 8;36
[PubMed:19591681]
[WorldCat.org]
[DOI]
(I e)