AccA

• Description: acetyl-CoA carboxylase (alpha subunit)
  
  

Gene name	accA
Synonyms
Essential	yes PubMed
Product	acetyl-CoA carboxylase (alpha subunit))
Function	production of malonyl-CoA, the substrate for fatty acid biosynthesis
Gene expression levels in SubtiExpress: accA
Interactions involving this protein in SubtInteract: AccA
Metabolic function and regulation of this protein in SubtiPathways: accA
MW, pI	36 kDa, 6.087
Gene length, protein length	975 bp, 325 aa
Immediate neighbours	pfkA, accD
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

• Locus tag: BSU29200

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU29200

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA (according to Swiss-Prot)

• Protein family: accA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

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

• Localization: cytoplasm (according to Swiss-Prot), Membrane-proximal (Spotty) PubMed

Database entries

• BsubCyc: BSU29200

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

• UniProt: O34847

• KEGG entry: [3]

• E.C. number: 6.4.1.2

Expression and regulation

• Operon: accD-accA PubMed

• Expression browser: accA PubMed

• Sigma factor:

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

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1031 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1470 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 795 PubMed

• • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 910 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)