Difference between revisions of "FabD"

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(References)
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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 17:56, 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
FabD context.gif
This image was kindly provided by SubtiList



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

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induced if the cells experience an accumulation of malonyl-CoA (FapR) PubMed
  • 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)

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)