Difference between revisions of "Des"
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=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' introduces double bonds into long chain fatty acids {{PubMed|21665975}} |
* '''Protein family:''' | * '''Protein family:''' | ||
Line 79: | Line 77: | ||
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
+ | ** [[Des]] receives electrons from ferredoxin ([[Fer]]) or from either of the two flavodoxins, [[YkuN]] or [[YkuP]], the three proteins can functionally replace each other {{PubMed|21665975}} | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
+ | ** [[Des]]-[[Fer]] (electron transfer to [[Des]]) {{PubMed|21665975}} | ||
+ | ** [[Des]]-[[YkuN]] (electron transfer to [[Des]]) {{PubMed|21665975}} | ||
+ | ** [[Des]]-[[YkuP]] (electron transfer to [[Des]]) {{PubMed|21665975}} | ||
− | * '''Localization:''' | + | * '''Localization:''' integral membrane protein {{PubMed|21665975}} |
=== Database entries === | === Database entries === | ||
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=References= | =References= | ||
− | <pubmed>19164152,11251847,12399512,9555904 10559169 11285232 , 12207704 12730185 19820084 12207704 20581210 </pubmed> | + | <pubmed>19164152,11251847,12399512,9555904 10559169 11285232 , 12207704 12730185 19820084 12207704 20581210 21665975 </pubmed> |
==Additional papers== | ==Additional papers== | ||
{{PubMed|18154726}} | {{PubMed|18154726}} | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:55, 1 July 2011
- Description: phospholipid desaturase
Gene name | des |
Synonyms | yocE |
Essential | no |
Product | phospholipid desaturase |
Function | adaptation of membrane fluidity at low temperatures |
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
MW, pI | 40 kDa, 9.88 |
Gene length, protein length | 1056 bp, 352 aa |
Immediate neighbours | yocD, desK |
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
lipid metabolism/ other, cold stress proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU19180
Phenotypes of a mutant
cold-sensitive PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: introduces double bonds into long chain fatty acids PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: integral membrane protein PubMed
Database entries
- Structure:
- UniProt: O34653
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: des PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Diego de Mendoza, Universidad Nacional de Rosario, Argentine homepage
Your additional remarks
References
Lorena Chazarreta-Cifre, Leticia Martiarena, Diego de Mendoza, Silvia G Altabe
Role of ferredoxin and flavodoxins in Bacillus subtilis fatty acid desaturation.
J Bacteriol: 2011, 193(16);4043-8
[PubMed:21665975]
[WorldCat.org]
[DOI]
(I p)
Jana Beranová, María C Mansilla, Diego de Mendoza, Dana Elhottová, Ivo Konopásek
Differences in cold adaptation of Bacillus subtilis under anaerobic and aerobic conditions.
J Bacteriol: 2010, 192(16);4164-71
[PubMed:20581210]
[WorldCat.org]
[DOI]
(I p)
Natalia Martin, Esteban Lombardía, Silvia G Altabe, Diego de Mendoza, María C Mansilla
A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis.
J Bacteriol: 2009, 191(24);7447-55
[PubMed:19820084]
[WorldCat.org]
[DOI]
(I p)
Anna-Barbara Hachmann, Esther R Angert, John D Helmann
Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin.
Antimicrob Agents Chemother: 2009, 53(4);1598-609
[PubMed:19164152]
[WorldCat.org]
[DOI]
(I p)
Silvia G Altabe, Pablo Aguilar, Gerardo M Caballero, Diego de Mendoza
The Bacillus subtilis acyl lipid desaturase is a delta5 desaturase.
J Bacteriol: 2003, 185(10);3228-31
[PubMed:12730185]
[WorldCat.org]
[DOI]
(P p)
Carsten L Beckering, Leif Steil, Michael H W Weber, Uwe Völker, Mohamed A Marahiel
Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis.
J Bacteriol: 2002, 184(22);6395-402
[PubMed:12399512]
[WorldCat.org]
[DOI]
(P p)
Larisa E Cybulski, Daniela Albanesi, María C Mansilla, Silvia Altabe, Pablo S Aguilar, Diego de Mendoza
Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase.
Mol Microbiol: 2002, 45(5);1379-88
[PubMed:12207704]
[WorldCat.org]
[DOI]
(P p)
P S Aguilar, A M Hernandez-Arriaga, L E Cybulski, A C Erazo, D de Mendoza
Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis.
EMBO J: 2001, 20(7);1681-91
[PubMed:11285232]
[WorldCat.org]
[DOI]
(P p)
M H Weber, W Klein, L Müller, U M Niess, M A Marahiel
Role of the Bacillus subtilis fatty acid desaturase in membrane adaptation during cold shock.
Mol Microbiol: 2001, 39(5);1321-9
[PubMed:11251847]
[WorldCat.org]
[DOI]
(P p)
P S Aguilar, P Lopez, D de Mendoza
Transcriptional control of the low-temperature-inducible des gene, encoding the delta5 desaturase of Bacillus subtilis.
J Bacteriol: 1999, 181(22);7028-33
[PubMed:10559169]
[WorldCat.org]
[DOI]
(P p)
P S Aguilar, J E Cronan, D de Mendoza
A Bacillus subtilis gene induced by cold shock encodes a membrane phospholipid desaturase.
J Bacteriol: 1998, 180(8);2194-200
[PubMed:9555904]
[WorldCat.org]
[DOI]
(P p)