A0A2R6XHN9 · A0A2R6XHN9_MARPO
- Proteinxanthine dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1404 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- xanthine + NAD+ + H2O = urate + NADH + 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 | 60 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 65 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 68 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 90 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 130 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 133 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 166 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 168 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | |||
Binding site | 321-328 | FAD (UniProtKB | ChEBI) | |||
Binding site | 401 | FAD (UniProtKB | ChEBI) | |||
Binding site | 411-415 | FAD (UniProtKB | ChEBI) | |||
Binding site | 424 | FAD (UniProtKB | ChEBI) | |||
Binding site | 468 | FAD (UniProtKB | ChEBI) | |||
Binding site | 486 | FAD (UniProtKB | ChEBI) | |||
Binding site | 839 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 870 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 874 | substrate | |||
Binding site | 952 | substrate | |||
Binding site | 984 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 986 | substrate | |||
Binding site | 1082 | substrate | |||
Binding site | 1151 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Active site | 1340 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | FAD binding | |
Molecular Function | iron ion binding | |
Molecular Function | xanthine dehydrogenase 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 > Viridiplantae > Streptophyta > Embryophyta > Marchantiophyta > Marchantiopsida > Marchantiidae > Marchantiales > Marchantiaceae > Marchantia
Accessions
- Primary accessionA0A2R6XHN9
Proteomes
Genome annotation databases
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-22 | Disordered | |||
Domain | 22-108 | 2Fe-2S ferredoxin-type | |||
Region | 235-277 | Disordered | |||
Compositional bias | 241-255 | Polar residues | |||
Compositional bias | 256-270 | Basic and acidic residues | |||
Domain | 293-478 | FAD-binding PCMH-type | |||
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,404
- Mass (Da)152,808
- Last updated2018-06-20 v1
- MD5 ChecksumB52E4511A7B3320675D13764F6125B85
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 241-255 | Polar residues | |||
Compositional bias | 256-270 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KZ772686 EMBL· GenBank· DDBJ | PTQ45617.1 EMBL· GenBank· DDBJ | Genomic DNA |