AcsA

• Description: acetyl-CoA synthetase
  
  

Gene name	acsA
Synonyms
Essential	no
Product	acetyl-CoA synthetase)
Function	utilization of acetate, fatty acids
Gene expression levels in SubtiExpress: acsA
Metabolic function and regulation of this protein in SubtiPathways: acsA
MW, pI	64 kDa, 5.547
Gene length, protein length	1716 bp, 572 aa
Immediate neighbours	ytzK, acuA
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

utilization of specific carbon sources, utilization of lipids

This gene is a member of the following regulons

CcpA regulon, CodY regulon

The gene

Basic information

• Locus tag: BSU29680

Database entries

• BsubCyc: BSU29680

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA (according to Swiss-Prot)

• Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: acetylated on Lys-549 by AcuA, this results in inactivation PubMed, deacetylated by SrtN and AcuC deacetylates (and thereby activates) AcsA PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU29680

• Structure:

• UniProt: P39062

• KEGG entry: [3]

• E.C. number: 6.2.1.1

Expression and regulation

• Operon: acsA PubMed

• Expression browser: acsA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (4.5-fold) (CcpA) PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • CodY: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 467 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 3357 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1384 PubMed

• • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3490 PubMed

Biological materials

• Mutant:
  • GP1212 (acsA::kan), available in Stülke lab
• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Eric L Hegg
Unraveling the structure and mechanism of acetyl-coenzyme A synthase.
Acc Chem Res: 2004, 37(10);775-83
[PubMed:15491124] [WorldCat.org] [DOI] (P p)

V J Starai, J C Escalante-Semerena
Acetyl-coenzyme A synthetase (AMP forming).
Cell Mol Life Sci: 2004, 61(16);2020-30
[PubMed:15316652] [WorldCat.org] [DOI] (P p)

Paul A Lindahl
Acetyl-coenzyme A synthase: the case for a Ni(p)(0)-based mechanism of catalysis.
J Biol Inorg Chem: 2004, 9(5);516-24
[PubMed:15221478] [WorldCat.org] [DOI] (P p)

Original publications

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Jeffrey G Gardner, Jorge C Escalante-Semerena
In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase.
J Bacteriol: 2009, 191(6);1749-55
[PubMed:19136592] [WorldCat.org] [DOI] (I p)

Jeffrey G Gardner, Jorge C Escalante-Semerena
Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in Bacillus subtilis.
J Bacteriol: 2008, 190(14);5132-6
[PubMed:18487328] [WorldCat.org] [DOI] (I p)

Boris R Belitsky, Abraham L Sonenshein
Genetic and biochemical analysis of CodY-binding sites in Bacillus subtilis.
J Bacteriol: 2008, 190(4);1224-36
[PubMed:18083814] [WorldCat.org] [DOI] (I p)

Uwe Linne, Antje Schäfer, Milton T Stubbs, Mohamed A Marahiel
Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains.
FEBS Lett: 2007, 581(5);905-10
[PubMed:17303131] [WorldCat.org] [DOI] (P p)

Jeffrey G Gardner, Frank J Grundy, Tina M Henkin, Jorge C Escalante-Semerena
Control of acetyl-coenzyme A synthetase (AcsA) activity by acetylation/deacetylation without NAD(+) involvement in Bacillus subtilis.
J Bacteriol: 2006, 188(15);5460-8
[PubMed:16855235] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

F J Grundy, A J Turinsky, T M Henkin
Catabolite regulation of Bacillus subtilis acetate and acetoin utilization genes by CcpA.
J Bacteriol: 1994, 176(15);4527-33
[PubMed:7913927] [WorldCat.org] [DOI] (P p)

F J Grundy, D A Waters, T Y Takova, T M Henkin
Identification of genes involved in utilization of acetate and acetoin in Bacillus subtilis.
Mol Microbiol: 1993, 10(2);259-71
[PubMed:7934817] [WorldCat.org] [DOI] (P p)