K7FHC8 · K7FHC8_PELSI
- ProteinD-amino-acid oxidase
- GeneDAO
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids344 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 | 37-38 | FAD (UniProtKB | ChEBI) | ||||
Sequence: DR | ||||||
Binding site | 44-45 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 49-51 | FAD (UniProtKB | ChEBI) | ||||
Sequence: AGL | ||||||
Binding site | 53 | D-dopa (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 179 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 214 | D-dopa (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 225 | D-dopa (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 280 | D-dopa (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 309-314 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GGFGLT | ||||||
Binding site | 310 | D-dopa (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | peroxisomal matrix | |
Cellular Component | presynaptic active zone | |
Molecular Function | D-amino-acid oxidase activity | |
Molecular Function | FAD binding | |
Molecular Function | identical protein binding | |
Biological Process | D-alanine catabolic process | |
Biological Process | D-serine catabolic process | |
Biological Process | dopamine biosynthetic 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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Trionychia > Trionychidae > Pelodiscus
Accessions
- Primary accessionK7FHC8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MRVAVIGAGVIGLSTA | ||||||
Chain | PRO_5003904182 | 17-344 | D-amino-acid oxidase | |||
Sequence: LCICDQYHSVIQPLEIEVYADRYTPLTTSDGAAGLWQPYLDDKENTQERVWNRETFDYLCGHLNSPEAEEMGLFLISGYNLFTQPVPEPPWKDIVLGFRNLTLKELELFPGYSYGWFNTALILEGKSYLPWLTQRLKKRGVKFFHKKIESFQEMGADVIINCTGVRAGDLQPDPGLMPGRGQIIKVLAPWVKHFVLTHDLKSGIYNSPYIIPGSKLVTLGGIFQLGNWNEENNPKDHKSIWENCCKLIPSLQKATIVDEWSGLRPVRYTVRLEREVVHHGSLKSEVIHNYGHGGFGLTIHWGCAMEAARIFGRILEEKKLAQSPPARL |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-325 | FAD dependent oxidoreductase | ||||
Sequence: RVAVIGAGVIGLSTALCICDQYHSVIQPLEIEVYADRYTPLTTSDGAAGLWQPYLDDKENTQERVWNRETFDYLCGHLNSPEAEEMGLFLISGYNLFTQPVPEPPWKDIVLGFRNLTLKELELFPGYSYGWFNTALILEGKSYLPWLTQRLKKRGVKFFHKKIESFQEMGADVIINCTGVRAGDLQPDPGLMPGRGQIIKVLAPWVKHFVLTHDLKSGIYNSPYIIPGSKLVTLGGIFQLGNWNEENNPKDHKSIWENCCKLIPSLQKATIVDEWSGLRPVRYTVRLEREVVHHGSLKSEVIHNYGHGGFGLTIHWGCAMEAAR |
Sequence similarities
Belongs to the DAMOX/DASOX family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)38,863
- Last updated2013-01-09 v1
- ChecksumF51E9FD50F51837F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7FHD7 | K7FHD7_PELSI | DAO | 332 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGCU01110774 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |