A0A5C6MZ15 · A0A5C6MZ15_9TELE
- ProteinD-amino-acid oxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids345 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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-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 + H2O2This 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
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 44-45 | FAD (UniProtKB | ChEBI) | |||
Binding site | 53 | D-dopa (UniProtKB | ChEBI) | |||
Binding site | 182 | FAD (UniProtKB | ChEBI) | |||
Binding site | 217 | D-dopa (UniProtKB | ChEBI) | |||
Binding site | 228 | D-serine (UniProtKB | ChEBI) | |||
Binding site | 283 | D-serine (UniProtKB | ChEBI) | |||
Binding site | 312-317 | FAD (UniProtKB | ChEBI) | |||
Binding site | 313 | D-serine (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | extracellular region | |
Cellular Component | peroxisomal matrix | |
Cellular Component | presynaptic active zone | |
Molecular Function | D-amino-acid oxidase activity | |
Molecular Function | FAD binding | |
Biological Process | D-alanine catabolic process | |
Biological Process | D-serine catabolic process | |
Biological Process | proline catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-amino-acid oxidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Tetraodontiformes > Tetradontoidea > Tetraodontidae > Takifugu
Accessions
- Primary accessionA0A5C6MZ15
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length345
- Mass (Da)38,775
- Last updated2019-11-13 v1
- Checksum4AF2B210111A6B0F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
RHFK02000018 EMBL· GenBank· DDBJ | TWW60402.1 EMBL· GenBank· DDBJ | Genomic DNA |