M1ZMM0 · M1ZMM0_DANRE
- Proteinxanthine dehydrogenase
- Geneaox5
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
Catalytic activity
- H2O + NAD+ + xanthine = H+ + NADH + urate
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 | 47 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 52 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 55 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 77 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 117 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 120 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 152 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 154 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 262-269 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LLVGNTTI | ||||||
Binding site | 365 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 409 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 427 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 773 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 804 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 918 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 920 | substrate | ||||
Sequence: F | ||||||
Binding site | 1086 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 1268 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | peroxisome | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | aldehyde oxidase activity | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | xanthine dehydrogenase activity | |
Molecular Function | xanthine oxidase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namexanthine dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionM1ZMM0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-95 | 2Fe-2S ferredoxin-type | ||||
Sequence: SELVFYINGKKIVEKNADPEEMLLAYLRRKVGLTGAKYGCGGGGCGACTVMVSRYDPLQDTVLHWSVNACLQPICSLHGAAVVTVEGI | ||||||
Domain | 234-419 | FAD-binding PCMH-type | ||||
Sequence: FQGEKVRWISPSDLKDLIKLKAEHSDAPLLVGNTTIGPKMNLNKTVHPLVIYGGSIAELQAIKWRKNCITVGAGCSLSVLKDVLQQRIEDLGPEKSRVYQALVQTLQCLAGKQIRNMATIGGNILSANPKYDLSSILAAAECTLHIASKDGDREICLSEEFFTDFGKTALRPEEILLAIDIPHSKP |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,336
- Mass (Da)147,202
- Last updated2013-05-01 v1
- Checksum85C1AA5B7EA8EE94
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX649296 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BK008657 EMBL· GenBank· DDBJ | DAA64406.1 EMBL· GenBank· DDBJ | mRNA |