A0A023X1V9 · A0A023X1V9_9ACTN

Function

function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site189-192CoA (UniProtKB | ChEBI)
Binding site307CoA (UniProtKB | ChEBI)
Binding site383-385ATP (UniProtKB | ChEBI)
Binding site407-412ATP (UniProtKB | ChEBI)
Binding site496ATP (UniProtKB | ChEBI)
Binding site511ATP (UniProtKB | ChEBI)
Binding site519CoA (UniProtKB | ChEBI)
Binding site522ATP (UniProtKB | ChEBI)
Binding site533Mg2+ (UniProtKB | ChEBI)
Binding site535Mg2+ (UniProtKB | ChEBI)
Binding site538Mg2+ (UniProtKB | ChEBI)
Binding site580CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionacetate-CoA ligase activity
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Biological Processacetyl-CoA biosynthetic process from acetate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acetyl-coenzyme A synthetase
  • EC number
  • Short names
    AcCoA synthetase
    ; Acs
  • Alternative names
    • Acetate--CoA ligase
    • Acyl-activating enzyme

Gene names

    • Name
      acsA
    • ORF names
      RradSPS_0746

Organism names

  • Taxonomic identifier
  • Strain
    • RSPS-4
  • Taxonomic lineage
    Bacteria > Actinomycetota > Rubrobacteria > Rubrobacterales > Rubrobacteraceae > Rubrobacter

Accessions

  • Primary accession
    A0A023X1V9

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue605N6-acetyllysine

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-24Disordered
Domain27-78Acetyl-coenzyme A synthetase N-terminal
Domain85-466AMP-dependent synthetase/ligase
Domain527-605AMP-binding enzyme C-terminal

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    643
  • Mass (Da)
    71,248
  • Last updated
    2014-07-09 v1
  • Checksum
    6C25262DC4739A0A
MSEEQTTPKLYEPPEEFASNANVSDPAVYEEAERDYKSFWAERARELHWFREWDEVLQWNPPEAKWFVGGKTNVAYNCLDYQIEQGRGDKVALVWEGDEPSDGTTYTYSELLAEVEKFANVLKSLGAEKGKPVSIYLPMIPELPVAMLACARIGAPHSIVFGAFSASALRDRINDCEATILVTADAAPRGGRKTPLKQNADEALEDAPSIENVVVVRRTGDDVPMQDGRDRYYDELMADAEESCPAEEMDSEDLLFILYSSGSTGKPKGIVHTTGGYLTQVNATTKWTMDLKDEDVYWCTADIGWITGHSYLVYGPLSAGGTSVQFEGTPAYPASDRWWDVIEKHKVTILYTAPTAIRSFMKGGTEDLEKHDLSSLRLLGTVGEPINPRAWEWYHENVGGGRCPIVDTWWQTETGGHMITPLPGITPTKPGSATRPFPGIEAGLFDEEGNEIEGEGSGNLVIKKPWPGMLRTLYKDPERYRETYWEKYGDVYFVGDGARRDEDGYYWITGRIDDVMNVSGHRISTAEVESALVGHPAVAESAVIGRADEDKGQAIVAYVILEGDREGSDELIQELNGQVRKVIGAHARPQEIIFTPDLPKTRSGKIMRRILRGVAEGQQDLGDTSTLADPSVVDALKESRAAN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007514
EMBL· GenBank· DDBJ
AHY46029.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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