Difference between revisions of "FabD"
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1MLA 1MLA] (the enzyme from ''E. coli'') {{PubMed|7768883}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P71019 P71019] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P71019 P71019] | ||
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<pubmed> 15952903 </pubmed> | <pubmed> 15952903 </pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| − | <pubmed>12737802, 16932747 19850612</pubmed> | + | <pubmed>12737802, 16932747 19850612 7768883 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:56, 6 January 2010
- 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
- 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
Reviews
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
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)
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)
