A0A2H4U2B6 · A0A2H4U2B6_EMEND
- Proteinxanthine dehydrogenase
- GenehxnS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1396 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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 | 49 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 54 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 57 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 78 | [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 | 161 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 163 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 312-319 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LVTGASEV | ||||||
Binding site | 397 | FAD (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 420 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 483 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 821 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 852 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 856 | substrate | ||||
Sequence: E | ||||||
Binding site | 934 | substrate | ||||
Sequence: R | ||||||
Binding site | 966 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 968 | substrate | ||||
Sequence: F | ||||||
Binding site | 1135 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 1327 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | oxidoreductase 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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA0A2H4U2B6
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-96 | 2Fe-2S ferredoxin-type | ||||
Sequence: PQLKFYLNGTPISLTSPHPRWTLLDFIRSQDGLKGTKLGCGEGGCGACTVVLQTRQHGKKIRHLAVNACLYPLIGVSGKHVITIEGL | ||||||
Region | 192-221 | Disordered | ||||
Sequence: LVGTEEETESDMGAHSGSGDTGSRSSGSCG | ||||||
Compositional bias | 205-219 | Polar residues | ||||
Sequence: AHSGSGDTGSRSSGS | ||||||
Domain | 284-473 | FAD-binding PCMH-type | ||||
Sequence: YGDAEQAWVKPRSVQEALEILSQCPSATLVTGASEVQVDVRFKDFRPSVSVFVGDITEMTGISWSEDMKTLYIGGSASLSDIEAECLRCIPLLKAVNLGSESVLSAIARTLRYFAGRQIRNAACLAGNIATASPISDMNPLLLAVGATVHARTSAEETTIPMSEMFKGYRKTALPSGSLITKIAVPMPSK |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,396
- Mass (Da)153,171
- Last updated2018-02-28 v1
- Checksum40E9F26977450407
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 205-219 | Polar residues | ||||
Sequence: AHSGSGDTGSRSSGS |