A0A562RIA3 · A0A562RIA3_9BRAD

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Protein has several cofactor binding sites:
Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Contains 1 topaquinone per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for active site.

166250100150200250300350400450500550600650
TypeIDPosition(s)Description
Active site310Proton acceptor
Active site394Schiff-base intermediate with substrate; via topaquinone

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 Functionaliphatic amine oxidase activity
Molecular Functioncopper ion binding
Molecular Functionprimary methylamine oxidase activity
Molecular Functionquinone binding
Biological Processamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Amine oxidase
  • EC number

Gene names

    • ORF names
      IQ16_03991

Organism names

  • Taxonomic identifier
  • Strain
    • CGMCC 1.10948
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium

Accessions

  • Primary accession
    A0A562RIA3

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue3942',4',5'-topaquinone

Post-translational modification

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.

Keywords

  • PTM
    • #TPQ

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-93AGAO-like N2
Domain108-212Copper amine oxidase N3-terminal
Domain234-635Copper amine oxidase catalytic

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    662
  • Mass (Da)
    73,650
  • Last updated
    2019-10-16 v1
  • Checksum
    4312C6A0C07D96F3
MLDTVKAKPQAQAAAPHPLDPLTAEEITAACTLVRAAATSPENCRFPTVRLEEPTKQELAAGGAGRRAFVLTLDVATGEAIEHIVDLSRGEIVARKIIPNREAPYGQPPVMLEEFFKCEAVVKADARWRAAMVRRGLSDKDIELVQVDPFSSGFFDKEFERGARIVRAVSYFREHLQDNGYAHPIEGVVAVVDLIGGEVIDLTDEDPIVPIPRKKRNYGAHELQNPRTDIKPLHIEQPEGASFRVDGWKVDWQKWSFRVGFTPREGLVLHQLAYQDGARKRSLIHRASVTEMVVPYADPTANHFWKSAFDAGEYGLGMLANALELGCDCIGNIHYFDVPAADGKGEPFVMQNAICMHEEDYGIAWKHYEFRNGLFEVRRSRRLVISFFATVGNYDYGFYWYLYQDGTIQLETKLTGIIQTAAVPSGETYRWGGMVDDNLGGPTHQHFFNVRLHMDLDGGGNTVTEHDFVPRPWGHDNPHGNVFDTTTRVLSRERDAAAVANGETGRFWKISNPNEINSVGNAPAYKLVVNPSPLMLAQEGSYVRKRGGFATKHVWVTAFDRDEKYASGDYPNVHAGGDGLPRYAAQNRNIENTDLVVWHSFGHTHVCKPEDFPIMPVEYAGFMLKPTGFFAANAAFDIPPERNSRSVLAGEGKGAASCCDKD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VLLA01000009
EMBL· GenBank· DDBJ
TWI68798.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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