Difference between revisions of "LcfA"
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− | * '''Description:''' long chain acyl-CoA synthetase <br/><br/> | + | * '''Description:''' long chain acyl-CoA synthetase, involved in surfactin production <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA (according to Swiss-Prot) | + | * '''Catalyzed reaction/ biological activity:''' ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA (according to Swiss-Prot), activates 3-hydroxy fatty acids for surfactin biosynthesis {{PubMed|20797616}} |
* '''Protein family:''' ATP-dependent AMP-binding enzyme family (according to Swiss-Prot) | * '''Protein family:''' ATP-dependent AMP-binding enzyme family (according to Swiss-Prot) | ||
− | * '''Paralogous protein(s):''' | + | * '''Paralogous protein(s):''' [[LcfB]], [[YhfT]], [[YngI]] |
=== Extended information on the protein === | === Extended information on the protein === | ||
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=Biological materials = | =Biological materials = | ||
− | * '''Mutant:''' | + | * '''Mutant:''' available in [[Mohamed Marahiel]]'s lab {{PubMed|20797616}} |
* '''Expression vector:''' | * '''Expression vector:''' | ||
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=References= | =References= | ||
− | <pubmed>17189250,17919287</pubmed> | + | <pubmed>17189250,17919287 20797616</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:21, 1 September 2010
- Description: long chain acyl-CoA synthetase, involved in surfactin production
Gene name | lcfA |
Synonyms | |
Essential | no |
Product | long chain acyl-CoA synthetase |
Function | fatty acid degradation |
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
MW, pI | 62 kDa, 6.119 |
Gene length, protein length | 1680 bp, 560 aa |
Immediate neighbours | fadR, yshE |
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: BSU28560
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA (according to Swiss-Prot), activates 3-hydroxy fatty acids for surfactin biosynthesis PubMed
- Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)
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: P94547
- KEGG entry: [3]
- E.C. number: 6.2.1.3
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant: available in Mohamed Marahiel's lab PubMed
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Femke I Kraas, Verena Helmetag, Melanie Wittmann, Matthias Strieker, Mohamed A Marahiel
Functional dissection of surfactin synthetase initiation module reveals insights into the mechanism of lipoinitiation.
Chem Biol: 2010, 17(8);872-80
[PubMed:20797616]
[WorldCat.org]
[DOI]
(I p)
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)