Difference between revisions of "AcsA"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1716 bp, 572 aa  
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1716 bp, 572 aa  
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[tyrS]]'', ''[[acuA]]''
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytzK]]'', ''[[acuA]]''
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14946&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14946&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''

Revision as of 09:20, 5 December 2012

  • Description: acetyl-CoA synthetase

Gene name acsA
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:
Central C-metabolism
MW, pI 64 kDa, 5.547
Gene length, protein length 1716 bp, 572 aa
Immediate neighbours ytzK, acuA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AcsA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AcsA expression.png

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

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

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

Biological materials

  • Mutant:
    • GP1212 (acsA::kan), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks



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)