AccD

• 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
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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]

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:

• Interactions:
  • (AccA-AccD)-AccB-AccC (acetyl-CoA carboxylase complex)

• Localization: Membrane-proximal (Spotty) PubMed Membrane-proximal (Spotty) PubMed

Database entries

• Structure: 1OD2 (carboxytransferase from yeast, equivalent to AccA-AccD) PubMed

• UniProt: C0SP93

• KEGG entry: [3]

• E.C. number: 6.4.1.2

Expression and regulation

• Operon: accD-accA (according to DBTBS)

• Expression browser: accD PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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)

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)