A1RR67 · A1RR67_PYRIL

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 site202-205CoA (UniProtKB | ChEBI)
Binding site323CoA (UniProtKB | ChEBI)
Binding site399-401ATP (UniProtKB | ChEBI)
Binding site423-428ATP (UniProtKB | ChEBI)
Binding site514ATP (UniProtKB | ChEBI)
Binding site529ATP (UniProtKB | ChEBI)
Binding site540ATP (UniProtKB | ChEBI)
Binding site551Mg2+ (UniProtKB | ChEBI)
Binding site553Mg2+ (UniProtKB | ChEBI)
Binding site556Mg2+ (UniProtKB | ChEBI)
Binding site598CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
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
    • Ordered locus names
      Pisl_0270

Organism names

Accessions

  • Primary accession
    A1RR67

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue623N6-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 domain.

TypeIDPosition(s)Description
Domain30-83Acetyl-coenzyme A synthetase N-terminal
Domain95-491AMP-dependent synthetase/ligase
Domain545-623AMP-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
    667
  • Mass (Da)
    76,141
  • Last updated
    2007-02-06 v1
  • Checksum
    AF3B6E82FB000AD0
MHQVLKEELPFNEYVINERWKSRLIDINAYKALHTKSLEQLEEFWASIARELEWFKPWDKVLDASNPPFYKWFVGGKLNLSYLALDRHVKTWRKNKLAIEWEGEPVDENGNPTEQRKLTYFDLYREVNRAAYMLKHNFGIRKGDRITLYMPMIPELPIVMLAAWRIGAVTSVVFSGFSAEALAERINDSQSRIVVTVDGFWRRGKVIRLKEIVDQALEKVGTVENVIVYRRLGLKDVPMTEGRDYWWHKVMEGIKANAYVEPEPLESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDLREEDIYWCTADIGWVTGHSYVVLGPLMIGATQVIYEGAPDYPQPDRWWAIIERYGVTILYTSPTAIRMFMRYGEEWPRRHDLSTLRIIHSVGEPINPEAWRWAYKVLGNENVAMASTWWMTETGGIVISHTPGLYLIPMKPGTNGLPLPGFDVDVFDDNGKPAPPGVRGYLVIKRPWPGMLHGIWGDPDRYIKTYWSKFPGVFYAGDYAIKDQDGYIWVLGRADEVIKVAGHRLGTYELESALVSHPTVAEAAVVGVPDPIKGEVPIAFVVLKQGVMPSDELRKELRDHVRKTIGPVAEPAHIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDTTTLEDETSVEEAKKAYEELRREIARG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000504
EMBL· GenBank· DDBJ
ABL87449.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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