Difference between revisions of "FabHB"
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* '''Regulation:''' | * '''Regulation:''' | ||
** induced if the cells experience a lack of malonyl-CoA ([[FapR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12737802 PubMed] | ** induced if the cells experience a lack of malonyl-CoA ([[FapR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12737802 PubMed] | ||
+ | ** induced upon fatty acid biosynthesis inhibition {{PubMed|21383089}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
Line 133: | Line 134: | ||
<pubmed> 15952903 17919287</pubmed> | <pubmed> 15952903 17919287</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
− | <pubmed>12737802,17114254,10629181, 10673437,19820084 </pubmed> | + | <pubmed>12737802,17114254,10629181, 10673437,19820084 21383089</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 15:40, 9 March 2011
- Description: beta-ketoacyl-acyl carrier protein synthase III
Gene name | fabHB |
Synonyms | yhfB , fabH2 |
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 | 35 kDa, 5.684 |
Gene length, protein length | 975 bp, 325 aa |
Immediate neighbours | yhgE, yhfC |
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: BSU10170
Phenotypes of a mutant
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: O07600
- KEGG entry: [3]
Additional information
- affinity for butyryl-CoA, but prefers acetyl-CoA in fatty acid biosynthesis PubMed
Expression and regulation
- Operon: fabHB PubMed
- 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
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
Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089]
[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)
Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254]
[WorldCat.org]
[DOI]
(P p)
Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802]
[WorldCat.org]
[DOI]
(P p)
C Davies, R J Heath, S W White, C O Rock
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Structure: 2000, 8(2);185-95
[PubMed:10673437]
[WorldCat.org]
[DOI]
(P p)
K H Choi, R J Heath, C O Rock
beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.
J Bacteriol: 2000, 182(2);365-70
[PubMed:10629181]
[WorldCat.org]
[DOI]
(P p)