A0A7J7E4H7 · A0A7J7E4H7_DICBM
- Proteinaldehyde oxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1444 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- an aldehyde + O2 + H2O = a carboxylate + H2O2 + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Note: Binds 2 [2Fe-2S] clusters.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 156 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 161 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 164 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 186 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 226 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 229 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 261 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 263 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 374-381 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LVMGNTAV | ||||||
Binding site | 477 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 539 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 882 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 913 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 1027 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1029 | substrate | ||||
Sequence: F | ||||||
Binding site | 1194 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 1375 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | aldehyde oxidase activity | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | NAD binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namealdehyde oxidase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7E4H7
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 346-531 | FAD-binding PCMH-type | ||||
Sequence: FLGERTTWITPVTLNDLLELKAKFPKAPLVMGNTAVGPSIKFTDEFHPVFISPLRLPELHFVDTTDDGVTIGAGYSLAQLNDALHFTVSEQPKEKTKTYRALLKHLRTLAGAQIRNMATLGGHVVSRPNFSDLNPILAAGNAVINLISKEGERQIPLDGHFLERSPEANLKPEEIVLSVYIPHSTP |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,444
- Mass (Da)160,783
- Last updated2021-04-07 v1
- Checksum0F9E63731744560C
Keywords
- Technical term