Difference between revisions of "FabHB"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1EBL 1EBL] (FabH from ''E. coli'') {{PubMed|10673437}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O07600 O07600] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O07600 O07600] | ||
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<pubmed> 15952903 17919287</pubmed> | <pubmed> 15952903 17919287</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| − | <pubmed>12737802,17114254,10629181, </pubmed> | + | <pubmed>12737802,17114254,10629181, 10673437 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:02, 6 January 2010
- Description: beta-ketoacyl-acyl carrier protein synthase III
| Gene name | fabHB |
| Synonyms | yhfB |
| Essential | no |
| Product | beta-ketoacyl-acyl carrier protein synthase III |
| Function | fatty acid biosynthesis |
| 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
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
Expression and regulation
- Operon: fabHB 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
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)
