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A2BGT3 · A2BGT3_DANRE

Function

Catalytic activity

  • D-alanine + O2 + H2O = pyruvate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-cysteine + O2 + H2O = 2-oxo-3-sulfanylpropanoate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-dopa + O2 + H2O = 3-(3,4-dihydroxyphenyl)pyruvate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-leucine + O2 + H2O = 4-methyl-2-oxopentanoate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-lysine + O2 + H2O = 6-amino-2-oxohexanoate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
    EC:1.4.3.3 (UniProtKB | ENZYME | Rhea)
  • D-methionine + O2 + H2O = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-phenylalanine + O2 + H2O = 3-phenylpyruvate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-proline + O2 = 1-pyrroline-2-carboxylate + H2O2
    This reaction proceeds in the forward direction.
  • D-serine + O2 + H2O = 3-hydroxypyruvate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-tryptophan + O2 + H2O = indole-3-pyruvate + H2O2 + NH4+
    This reaction proceeds in the forward direction.
  • D-valine + O2 + H2O = 3-methyl-2-oxobutanoate + H2O2 + NH4+
    This reaction proceeds in the forward direction.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site44-45FAD (UniProtKB | ChEBI)
Binding site53D-dopa (UniProtKB | ChEBI)
Binding site217D-dopa (UniProtKB | ChEBI)
Binding site228D-serine (UniProtKB | ChEBI)
Binding site283D-serine (UniProtKB | ChEBI)
Binding site312-317FAD (UniProtKB | ChEBI)
Binding site313D-serine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell projection
Cellular Componentcytoplasm
Cellular Componentextracellular region
Cellular Componentperoxisomal matrix
Cellular Componentpresynaptic active zone
Molecular FunctionD-amino-acid oxidase activity
Molecular FunctionFAD binding
Biological ProcessD-alanine catabolic process
Biological ProcessD-serine catabolic process
Biological Processproline catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    D-amino-acid oxidase
  • EC number

Gene names

    • Name
      dao.1
    • Synonyms
      wu:fb55b11
      , zgc:113922

Organism names

  • Taxonomic identifier
  • Strain
    • Tuebingen
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    A2BGT3
  • Secondary accessions
    • A0A8M2BCE8
    • E7F7N4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-329FAD dependent oxidoreductase

Sequence similarities

Belongs to the DAMOX/DASOX family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    348
  • Mass (Da)
    39,346
  • Last updated
    2007-02-20 v1
  • MD5 Checksum
    54D3ABF53A7744927EAAABD91805B5AA
MRVCIIGAGVIGLSTAQSIYQHFHSRVSPLTIEVYADIFTPLTTSDGAAGFWQPYLYDKGNVKETQWNKETFNYLLSFLNSPDSIKMGIFLESGYNLCFEPMPEPSFKQAVLGFRQLSKRELEMFPGFSFGWFNTALVIEGKSYLPWLMDWLNQRGVKFFQRKIDSFKELSDSGADMIINCSGVRSGDLQPDPELQPARGQIIKVDAPWLKHWVITHDSKLGTYNTPYIIPGSRLVTVGGVFQVGNWNRMNSSVEHKQIWEGACKLEPSLQHARIVEDWTGLRPARSKVRLERESIRCGGHSFEVIHNYGHGGFGLTIHRGCAEEAARLFGQFLEQKGLLTSQAKSRL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
Q4V981Q4V981_DANREdao.1348

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX511005
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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