Difference between revisions of "AcsA"

From SubtiWiki
Jump to: navigation, search
(Reviews)
Line 145: Line 145:
 
=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed> 15316652 15491124 15221478 </pubmed>
+
<pubmed> 15316652 15491124 15221478 22900538 </pubmed>
 +
 
 
==Original publications==
 
==Original publications==
 
<pubmed>7934817,7913927,18083814,17303131,12618455,19136592, 18487328, 12850135 16855235</pubmed>
 
<pubmed>7934817,7913927,18083814,17303131,12618455,19136592, 18487328, 12850135 16855235</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:26, 21 August 2012

  • 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:
Central C-metabolism
MW, pI 64 kDa, 5.547
Gene length, protein length 1716 bp, 572 aa
Immediate neighbours tyrS, 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

References

Reviews

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)

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