K7FHC8 · K7FHC8_PELSI

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 site37-38FAD (UniProtKB | ChEBI)
Binding site44-45FAD (UniProtKB | ChEBI)
Binding site49-51FAD (UniProtKB | ChEBI)
Binding site53D-dopa (UniProtKB | ChEBI)
Binding site179FAD (UniProtKB | ChEBI)
Binding site214D-dopa (UniProtKB | ChEBI)
Binding site225D-dopa (UniProtKB | ChEBI)
Binding site280D-dopa (UniProtKB | ChEBI)
Binding site309-314FAD (UniProtKB | ChEBI)
Binding site310D-dopa (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell projection
Cellular Componentcytosol
Cellular Componentextracellular region
Cellular Componentmitochondrial outer membrane
Cellular Componentperoxisomal matrix
Cellular Componentpresynaptic active zone
Molecular FunctionD-amino-acid oxidase activity
Molecular FunctionFAD binding
Molecular Functionidentical protein binding
Biological ProcessD-alanine catabolic process
Biological ProcessD-serine catabolic process
Biological Processdopamine biosynthetic 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

Organism names

Accessions

  • Primary accession
    K7FHC8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-16
ChainPRO_500390418217-344D-amino-acid oxidase

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-325FAD dependent oxidoreductase

Sequence similarities

Belongs to the DAMOX/DASOX family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    344
  • Mass (Da)
    38,863
  • Last updated
    2013-01-09 v1
  • Checksum
    F51E9FD50F51837F
MRVAVIGAGVIGLSTALCICDQYHSVIQPLEIEVYADRYTPLTTSDGAAGLWQPYLDDKENTQERVWNRETFDYLCGHLNSPEAEEMGLFLISGYNLFTQPVPEPPWKDIVLGFRNLTLKELELFPGYSYGWFNTALILEGKSYLPWLTQRLKKRGVKFFHKKIESFQEMGADVIINCTGVRAGDLQPDPGLMPGRGQIIKVLAPWVKHFVLTHDLKSGIYNSPYIIPGSKLVTLGGIFQLGNWNEENNPKDHKSIWENCCKLIPSLQKATIVDEWSGLRPVRYTVRLEREVVHHGSLKSEVIHNYGHGGFGLTIHWGCAMEAARIFGRILEEKKLAQSPPARL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
K7FHD7K7FHD7_PELSIDAO332

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCU01110774
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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