Difference between revisions of "FadE"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU32820&redirect=T BSU32820] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yusMLKJ.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yusMLKJ.html] | ||
Line 93: | Line 94: | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU32820&redirect=T BSU32820] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=2Z1Q 2Z1Q] (from ''Thermus thermophilus hb8'', 52% identity, 68% similarity) | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=2Z1Q 2Z1Q] (from ''Thermus thermophilus hb8'', 52% identity, 68% similarity) |
Revision as of 14:42, 2 April 2014
- Description: acyl-CoA dehydrogenase
Gene name | fadE |
Synonyms | yusJ |
Essential | no |
Product | acyl-CoA dehydrogenase |
Function | fatty acid degradation |
Gene expression levels in SubtiExpress: fadE | |
Metabolic function and regulation of this protein in SubtiPathways: fadE | |
MW, pI | 65 kDa, 5.146 |
Gene length, protein length | 1782 bp, 594 aa |
Immediate neighbours | yusI, fadA |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed 500px |
Contents
Categories containing this gene/protein
utilization of lipids, membrane proteins
This gene is a member of the following regulons
CcpA regulon, FadR regulon, SdpR regulon
The gene
Basic information
- Locus tag: BSU32820
Phenotypes of a mutant
Database entries
- BsubCyc: BSU32820
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF (according to Swiss-Prot)
- Protein family: acyl-CoA dehydrogenase family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane PubMed
Database entries
- BsubCyc: BSU32820
- Structure: 2Z1Q (from Thermus thermophilus hb8, 52% identity, 68% similarity)
- UniProt: O32176
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921]
[WorldCat.org]
[DOI]
(I p)
Shigeo Tojo, Takenori Satomura, Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Catabolite repression of the Bacillus subtilis FadR regulon, which is involved in fatty acid catabolism.
J Bacteriol: 2011, 193(10);2388-95
[PubMed:21398533]
[WorldCat.org]
[DOI]
(I p)
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation.
J Biol Chem: 2007, 282(8);5180-94
[PubMed:17189250]
[WorldCat.org]
[DOI]
(P p)
José E González-Pastor, Errett C Hobbs, Richard Losick
Cannibalism by sporulating bacteria.
Science: 2003, 301(5632);510-3
[PubMed:12817086]
[WorldCat.org]
[DOI]
(I p)