Difference between revisions of "FabF"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1OX0 1OX0] (the protein from ''Streptococcus pneumoniae'') {{PubMed|12837788}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34340 O34340] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O34340 O34340] | ||
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<pubmed> 15952903 17919287</pubmed> | <pubmed> 15952903 17919287</pubmed> | ||
==Original Publications== | ==Original Publications== | ||
− | <pubmed>18384517,,12737802, </pubmed> | + | <pubmed>18384517, 12837788,12737802, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:05, 6 January 2010
- Description: beta-ketoacyl-acyl carrier protein synthase II
Gene name | fabF |
Synonyms | yjaY |
Essential | yes PubMed |
Product | beta-ketoacyl-acyl carrier protein synthase II |
Function | fatty acid biosynthesis |
MW, pI | 43 kDa, 4.768 |
Gene length, protein length | 1239 bp, 413 aa |
Immediate neighbours | fabHA, yjaZ |
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: BSU11340
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein] (according to Swiss-Prot)
- Protein family: beta-ketoacyl-ACP synthases family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: O34340
- KEGG entry: [3]
- E.C. number: 2.3.1.179
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
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
Gustavo E Schujman, Silvia Altabe, Diego de Mendoza
A malonyl-CoA-dependent switch in the bacterial response to a dysfunction of lipid metabolism.
Mol Microbiol: 2008, 68(4);987-96
[PubMed:18384517]
[WorldCat.org]
[DOI]
(I p)
Allen C Price, Charles O Rock, Stephen W White
The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae.
J Bacteriol: 2003, 185(14);4136-43
[PubMed:12837788]
[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)