Q8AAN6 · Q8AAN6_BACTN

Function

function

Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).

Catalytic activity

Pathway

Aromatic compound metabolism; phenylacetate degradation.

Features

Showing features for binding site.

143550100150200250300350400
TypeIDPosition(s)Description
Binding site94ADP 1 (UniProtKB | ChEBI)
Binding site165CoA (UniProtKB | ChEBI)
Binding site166CoA (UniProtKB | ChEBI)
Binding site190CoA (UniProtKB | ChEBI)
Binding site214ADP 2 (UniProtKB | ChEBI)
Binding site214ADP 1 (UniProtKB | ChEBI)
Binding site214AMP 2 (UniProtKB | ChEBI)
Binding site214AMP 1 (UniProtKB | ChEBI)
Binding site235ADP 2 (UniProtKB | ChEBI)
Binding site235ADP 1 (UniProtKB | ChEBI)
Binding site235AMP 2 (UniProtKB | ChEBI)
Binding site235AMP 1 (UniProtKB | ChEBI)
Binding site236ADP 1 (UniProtKB | ChEBI)
Binding site236ADP 2 (UniProtKB | ChEBI)
Binding site236AMP 1 (UniProtKB | ChEBI)
Binding site236AMP 2 (UniProtKB | ChEBI)
Binding site238ADP 1 (UniProtKB | ChEBI)
Binding site238AMP 1 (UniProtKB | ChEBI)
Binding site240ADP 3 (UniProtKB | ChEBI)
Binding site240ADP 1 (UniProtKB | ChEBI)
Binding site240ADP 2 (UniProtKB | ChEBI)
Binding site240AMP 2 (UniProtKB | ChEBI)
Binding site240AMP 1 (UniProtKB | ChEBI)
Binding site251Zn2+ (UniProtKB | ChEBI)
Binding site258Zn2+ (UniProtKB | ChEBI)
Binding site304ADP 1 (UniProtKB | ChEBI)
Binding site304ADP 3 (UniProtKB | ChEBI)
Binding site304ADP 2 (UniProtKB | ChEBI)
Binding site304AMP 1 (UniProtKB | ChEBI)
Binding site304AMP 2 (UniProtKB | ChEBI)
Binding site313Zn2+ (UniProtKB | ChEBI)
Binding site315Zn2+ (UniProtKB | ChEBI)
Binding site328ADP 2 (UniProtKB | ChEBI)
Binding site328ADP 1 (UniProtKB | ChEBI)
Binding site328ADP 3 (UniProtKB | ChEBI)
Binding site328AMP 2 (UniProtKB | ChEBI)
Binding site328AMP 1 (UniProtKB | ChEBI)
Binding site336CoA (UniProtKB | ChEBI)
Binding site339ADP 2 (UniProtKB | ChEBI)
Binding site339ADP 3 (UniProtKB | ChEBI)
Binding site339AMP 2 (UniProtKB | ChEBI)
Binding site407CoA (UniProtKB | ChEBI)
Binding site424ADP 1 (UniProtKB | ChEBI)
Binding site424AMP 1 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
Molecular Functionphenylacetate-CoA ligase activity
Biological Processphenylacetate catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phenylacetate-coenzyme A ligase
  • EC number
  • Alternative names
    • Phenylacetyl-CoA ligase

Gene names

    • Ordered locus names
      BT_0428

Organism names

Accessions

  • Primary accession
    Q8AAN6

Proteomes

PTM/Processing

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain93-287AMP-dependent synthetase/ligase
Domain337-432AMP-dependent ligase C-terminal

Sequence similarities

Belongs to the phenylacetyl-CoA ligase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    435
  • Mass (Da)
    49,380
  • Last updated
    2003-06-01 v1
  • Checksum
    50F97E048724D7A2
MSTQYWEEEIEIMSREKLQELQLQRLKKTINIAANSPYYKEVFSKNGITGDSIQSLDDIRKIPFTTKSDMRANYPFGLVAGDMKRDGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGPGVAFECQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIRYRTRDLTRILPGKCPCGRTHLRIDRIKGRSDDMFIIKGVNIFPMQVEKILVQFPELGSNYLITLETVNNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQLKDEILVTPKVKLVKKGSLPQSEGKAVRVKDLRDNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE015928
EMBL· GenBank· DDBJ
AAO75535.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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