FabD
-  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 | 
|  Metabolic function and regulation of this protein in SubtiPathways:  Lipid synthesis  | |
| 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
- UniProt: P71019
 
- KEGG entry: [3]
 
- E.C. number: 2.3.1.39
 
Additional information
Expression and regulation
- Regulation:
 
- Regulatory mechanism:
 
- 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
Original Publications
Mariano A Martinez, Diego de Mendoza, Gustavo E Schujman  
Transcriptional and functional characterization of the gene encoding acyl carrier protein in Bacillus subtilis. 
Microbiology (Reading): 2010, 156(Pt 2);484-495 
[PubMed:19850612]
  [WorldCat.org]
 [DOI]
 (I p)
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)
Natalia Comella, Alan D Grossman  
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis. 
Mol Microbiol: 2005, 57(4);1159-74 
[PubMed:16091051]
  [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)
L Serre, E C Verbree, Z Dauter, A R Stuitje, Z S Derewenda  
The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component. 
J Biol Chem: 1995, 270(22);12961-4 
[PubMed:7768883]
  [WorldCat.org]
 [DOI]
 (P p)
