A6IP50 · A6IP50_RAT
- Proteinaldehyde oxidase
- GeneAox1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1333 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- H2O + O2 + retinal = H+ + H2O2 + retinoate
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 | 43 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 48 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 51 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 73 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 113 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 116 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 148 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 150 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 263-270 | FAD (UniProtKB | ChEBI) | ||||
Sequence: IVMGYTSV | ||||||
Binding site | 366 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 410 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 428 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 771 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 802 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 916 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 918 | substrate | ||||
Sequence: F | ||||||
Binding site | 1083 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 1265 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | molybdopterin cofactor binding | |
Molecular Function | NAD binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | lipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namealdehyde oxidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionA6IP50
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-91 | 2Fe-2S ferredoxin-type | ||||
Sequence: PQLLFYVNGQKVVENNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKSIRHHPVNACLTPICSLYGTAVTTVEGI | ||||||
Domain | 235-420 | FAD-binding PCMH-type | ||||
Sequence: FYSNRMTWISPVTLEELVEAKFKYPGAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELSIINQTGDGLTLGAGLSLDQVKDILTDVVQKLPEETTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGKRQIPLSEQFLRKCPDSDLKPQEVLVSVNIPCSRK |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,333
- Mass (Da)146,898
- Last updated2023-06-28 v1
- ChecksumCFBB85D327B11F3F