Difference between revisions of "AcdA"
Line 1: | Line 1: | ||
− | + | * '''Description:''' acyl-CoA dehydrogenase <br/><br/> | |
− | |||
− | |||
− | |||
− | |||
− | |||
− | |||
− | |||
− | * '''Description:''' acyl-CoA dehydrogenase | ||
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
Line 22: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || fatty acid degradation | |style="background:#ABCDEF;" align="center"|'''Function''' || fatty acid degradation | ||
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_deg.html Fatty acid degradation]''' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 41 kDa, 4.951 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 41 kDa, 4.951 | ||
Line 30: | Line 22: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rpoE]]'', ''[[fadF]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rpoE]]'', ''[[fadF]]'' | ||
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+& | + | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB15745]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
|- | |- | ||
− | |colspan="2" | '''Genetic context''' | + | |colspan="2" | '''Genetic context''' <br/> [[Image:acdA_context.gif]] |
− | + | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | |
|- | |- | ||
|} | |} | ||
Line 39: | Line 31: | ||
__TOC__ | __TOC__ | ||
− | + | <br/><br/><br/><br/><br/><br/> | |
=The gene= | =The gene= | ||
Line 129: | Line 121: | ||
=References= | =References= | ||
− | + | <pubmed>17189250,17919287</pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 05:15, 24 November 2010
- Description: acyl-CoA dehydrogenase
Gene name | acdA |
Synonyms | |
Essential | no |
Product | acyl-CoA dehydrogenase |
Function | fatty acid degradation |
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
MW, pI | 41 kDa, 4.951 |
Gene length, protein length | 1137 bp, 379 aa |
Immediate neighbours | rpoE, fadF |
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: BSU37170
Phenotypes of a mutant
Database entries
- 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:
- Interactions:
- Localization:
Database entries
- Structure: 2Z1Q (from Thermus thermophilus hb8, 40% identity, 55% similarity)
- UniProt: P45867
- KEGG entry: [3]
- E.C. number:
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
Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287]
[WorldCat.org]
[DOI]
(P 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)