C4R4G9 · OXDA_KOMPG
- ProteinD-amino-acid oxidase
- GeneDAO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids344 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:20550580).
Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:20550580).
Enables the organism to utilize D-alanine as a source of nitrogen (PubMed:20550580).
Enables the organism to utilize D-amino acids as a source of nutrients (PubMed:20550580).
Enables the organism to utilize D-alanine as a source of nitrogen (PubMed:20550580).
Catalytic activity
- a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4+This reaction proceeds in the forward direction.
- D-alanine + H2O + O2 = H2O2 + NH4+ + pyruvateThis reaction proceeds in the forward direction.
Cofactor
pH Dependence
Optimum pH is 9.6.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 14 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 49 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 53 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 55 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 167 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 229 | (R)-lactate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 229 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 290 | (R)-lactate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 290 | anthranilate 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 290 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 321 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 324 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 325 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 326 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisomal matrix | |
Cellular Component | peroxisome | |
Molecular Function | D-amino-acid oxidase activity | |
Molecular Function | FAD binding | |
Biological Process | D-alanine metabolic process | |
Biological Process | D-amino acid metabolic process | |
Biological Process | D-valine metabolic process | |
Biological Process | nitrogen utilization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-amino-acid oxidase
- EC number
- Short namesDAAO ; DAMOX ; DAO
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Phaffomycetaceae > Komagataella
Accessions
- Primary accessionC4R4G9
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Unable to utilize D-alanine as a nitrogen source.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000460036 | 1-344 | D-amino-acid oxidase | |||
Sequence: MTDSKYVIIGAGISGLYTAWSLIDKGTGPSDIKVVAEFLPGDQSTLYTSPWAGGNFSLITSTDERSMKFDKFTYTNLHRIQELLGGPECGLDMLPSTEMFEQELDHAKLDSISQYLKEYRPMTKEEMPEGVVSGVKFLTWNFNCPLFLANFQKHLAAIGVTFERSKIDHISSVFSPSVDAVFNCTGIGAASLGGVKDENVFPTRGQVVVVRAPHIRENRFRWRPDSDTYVIPRPFSDGSIVMGGFFQEGNWSGNTYGYETEDILKRGLELYPEIGKRNELKIIREAAGLRPSRKGGVRIEVEHFDQVNGKDRYIVHNYGASGYGYQSGLGMANEATDMYFEAAK |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)38,343
- Last updated2009-07-07 v1
- Checksum62AF95C94884B5E0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FN392321 EMBL· GenBank· DDBJ | CAY70455.1 EMBL· GenBank· DDBJ | Genomic DNA |