Difference between revisions of "FabG"

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(References)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1I01 1I01] (the enzyme from ''E. coli'') {{PubMed|11669613}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P51831 P51831]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P51831 P51831]
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<pubmed> 15952903 17919287</pubmed>
 
<pubmed> 15952903 17919287</pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>12737802, 16932747 19850612</pubmed>
+
<pubmed>12737802, 16932747 19850612 11669613 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:22, 6 January 2010

  • Description: beta-ketoacyl-acyl carrier protein reductase

Gene name fabG
Synonyms ylpF
Essential yes PubMed
Product beta-ketoacyl-acyl carrier protein reductase
Function fatty acid biosynthesis
MW, pI 26 kDa, 8.091
Gene length, protein length 738 bp, 246 aa
Immediate neighbours fabD, acpA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FabG context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU15910

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: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH (according to Swiss-Prot)
  • Protein family: short-chain dehydrogenases/reductases (SDR) 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: 1I01 (the enzyme from E. coli) PubMed
  • 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

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

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)

A C Price, Y M Zhang, C O Rock, S W White
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Biochemistry: 2001, 40(43);12772-81
[PubMed:11669613] [WorldCat.org] [DOI] (P p)