Difference between revisions of "FabHA"
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| − | * '''Description:''' beta-ketoacyl-acyl carrier protein synthase III <br/><br/> | + | * '''Description:''' beta-ketoacyl-acyl carrier protein synthase III, principal condensing enzyme responsible for the initiation of fatty acid synthesis in non-stressed ''B. subtilis'' cells <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| + | * significant increase in the proportion of straight-chain fatty acids with a concomitant increase in 31:0-carbon phosphatidylethanolamine species {{PubMed|21542858}} | ||
=== Database entries === | === Database entries === | ||
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=== Additional information=== | === Additional information=== | ||
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** inhibited by cerulenin {{PubMed|11325930}} | ** inhibited by cerulenin {{PubMed|11325930}} | ||
** induced upon fatty acid biosynthesis inhibition {{PubMed|21383089}} | ** induced upon fatty acid biosynthesis inhibition {{PubMed|21383089}} | ||
| + | ** expression is reduced when [[SigW]] is activated (by alkaline shock, polymyxin B, vancomycin, cephalosporin C, D-cycloserine, and triton X-100) {{PubMed|21542858}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| Line 137: | Line 137: | ||
<pubmed> 15952903 17919287</pubmed> | <pubmed> 15952903 17919287</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| + | '''Additional publications:''' {{PubMed|21542858}} | ||
<pubmed>12737802,17114254,10629181, 10673437,19820084 21383089</pubmed> | <pubmed>12737802,17114254,10629181, 10673437,19820084 21383089</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 15:16, 6 May 2011
- Description: beta-ketoacyl-acyl carrier protein synthase III, principal condensing enzyme responsible for the initiation of fatty acid synthesis in non-stressed B. subtilis cells
| Gene name | fabHA |
| Synonyms | yjaX , fabH1 |
| Essential | no |
| Product | beta-ketoacyl-acyl carrier protein synthase III |
| Function | fatty acid biosynthesis |
| Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis | |
| MW, pI | 33 kDa, 5.045 |
| Gene length, protein length | 936 bp, 312 aa |
| Immediate neighbours | yjzB, fabF |
| 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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU11330
Phenotypes of a mutant
- significant increase in the proportion of straight-chain fatty acids with a concomitant increase in 31:0-carbon phosphatidylethanolamine species PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2 (according to Swiss-Prot)
- Protein family: fabH 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
- UniProt: O34746
- KEGG entry: [3]
Additional information
- affinity for butyryl-CoA, but prefers acetyl-CoA in fatty acid biosynthesis PubMed
Expression and regulation
- Regulation:
- expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
- inhibited by cerulenin PubMed
- induced upon fatty acid biosynthesis inhibition PubMed
- expression is reduced when SigW is activated (by alkaline shock, polymyxin B, vancomycin, cephalosporin C, D-cycloserine, and triton X-100) PubMed
- 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
Reviews
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)
Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903]
[WorldCat.org]
[DOI]
(P p)
Original Publications
Additional publications: PubMed
