Difference between revisions of "FabD"
| Line 90: | Line 90: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[fapR]]-[[plsX]]-[[fabD]]-[[fabG]]'' {{PubMed|12737802}} |
| − | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|16932747}} |
* '''Regulation:''' | * '''Regulation:''' | ||
| − | ** repressed unless the cells experience | + | ** repressed unless the cells experience an accumulation of malonyl-CoA ([[FapR]]) {{PubMed|12737802}} |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | ** [[FapR]]: transcription repression | + | ** [[FapR]]: transcription repression {{PubMed|12737802}} |
* '''Additional information:''' | * '''Additional information:''' | ||
| Line 122: | Line 122: | ||
=References= | =References= | ||
| − | <pubmed>12737802, </pubmed> | + | <pubmed>12737802, 16932747</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 17:00, 11 October 2009
- Description: malonyl CoA-acyl carrier protein transacylase
| Gene name | fabD |
| Synonyms | ylpE |
| Essential | yes PubMed |
| Product | malonyl CoA-acyl carrier protein transacylase |
| Function | fatty acid biosynthesis |
| MW, pI | 33 kDa, 4.515 |
| Gene length, protein length | 951 bp, 317 aa |
| Immediate neighbours | plsX, fabG |
| 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: BSU15900
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: Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein] (according to Swiss-Prot)
- Protein family: fabD 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
- Structure:
- UniProt: P71019
- KEGG entry: [3]
- E.C. number: 2.3.1.39
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
Gustavo E Schujman, Marcelo Guerin, Alejandro Buschiazzo, Francis Schaeffer, Leticia I Llarrull, Georgina Reh, Alejandro J Vila, Pedro M Alzari, Diego de Mendoza
Structural basis of lipid biosynthesis regulation in Gram-positive bacteria.
EMBO J: 2006, 25(17);4074-83
[PubMed:16932747]
[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)
