Difference between revisions of "AccD"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1OD2 1OD2] (carboxytransferase from yeast, equivalent to [[AccA]]-[[AccD]]) {{PubMed|12663926}}
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* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=2F9I 2F9I] (from ''Staphylococcus aureus''; equivalent to [[AccD]]-[[AccA]], 64% identity) {{PubMed|16460018}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/C0SP93 C0SP93]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/C0SP93 C0SP93]
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<pubmed> 15952903 </pubmed>
 
<pubmed> 15952903 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>15066985, 12663926,14651647,16479537 22517742 22383849</pubmed>
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<pubmed>15066985, 12663926,14651647,16479537 22517742 22383849 16460018</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:14, 12 July 2013

  • Description: acetyl-CoA carboxylase (beta subunit)

Gene name accD
Synonyms yttI
Essential yes PubMed
Product acetyl-CoA carboxylase (beta subunit))
Function production of malonyl-CoA, the substrate for fatty acid biosynthesis
Gene expression levels in SubtiExpress: accD
Interactions involving this protein in SubtInteract: AccD
Metabolic function and regulation of this protein in SubtiPathways:
Lipid synthesis
MW, pI 28 kDa, 5.344
Gene length, protein length 786 bp, 262 aa
Immediate neighbours accA, ytsJ
Sequences Protein DNA DNA_with_flanks
Genetic context
AccD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AccD expression.png















Categories containing this gene/protein

biosynthesis of lipids, essential genes, phosphoproteins

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

  • Locus tag: BSU29210

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:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-205 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2F9I (from Staphylococcus aureus; equivalent to AccD-AccA, 64% identity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • expressed under conditions that trigger sporulation (Spo0A) 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

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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Patrick Bilder, Sandra Lightle, Graeme Bainbridge, Jeffrey Ohren, Barry Finzel, Fang Sun, Susan Holley, Loola Al-Kassim, Cindy Spessard, Michael Melnick, Marcia Newcomer, Grover L Waldrop
The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
Biochemistry: 2006, 45(6);1712-22
[PubMed:16460018] [WorldCat.org] [DOI] (P p)

Christoph Freiberg, Nina A Brunner, Guido Schiffer, Thomas Lampe, Jens Pohlmann, Michael Brands, Martin Raabe, Dieter Häbich, Karl Ziegelbauer
Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity.
J Biol Chem: 2004, 279(25);26066-73
[PubMed:15066985] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Hailong Zhang, Zhiru Yang, Yang Shen, Liang Tong
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
Science: 2003, 299(5615);2064-7
[PubMed:12663926] [WorldCat.org] [DOI] (I p)