P91711 · XDH_DROSU
- ProteinXanthine dehydrogenase
- GeneXdh
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1344 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity).
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 per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 56 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 78 | [2Fe-2S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 118 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 121 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 153 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 155 | [2Fe-2S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 264-271 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LVVGNTEV | ||||||
Binding site | 344 | FAD (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 354-358 | FAD (UniProtKB | ChEBI) | ||||
Sequence: CLGGN | ||||||
Binding site | 367 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 433 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 781 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 812 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 816 | substrate | ||||
Sequence: E | ||||||
Binding site | 894 | substrate | ||||
Sequence: R | ||||||
Binding site | 926 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 928 | substrate | ||||
Sequence: F | ||||||
Binding site | 1093 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 1276 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | FAD binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | iron ion binding | |
Molecular Function | molybdopterin cofactor binding | |
Molecular Function | xanthine dehydrogenase activity | |
Biological Process | xanthine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameXanthine dehydrogenase
- EC number
- Short namesXD
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP91711
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000166081 | 1-1344 | Xanthine dehydrogenase | |||
Sequence: MSGQQQATSVLVFFVNGKKVTDTNPDPECTLLTYLRDKLRLCGTKLGCAEGGCGACTVMISRMDRGQHKIRHLAVNACLTPVCAMHGCAVTTVEGIGSTRTRLHPVQERLAKAHGSQCGFCTPGIVMSMYALLRNAEQPSMRDLEVAFQGNLCRCTGYRPILEGYKTFTKEFLCGMGEKCCRVNGKGCGGGDDPESVTDDTLFERSKFQPLDASQEPIFPPELQLSNAYDSESLVFSSERVTWYRPTTLQELLQLKAAHPAAKLVVGNTEVGVEVKFKHFLYPHLINPTLVAELQEVRESEESIYFGAAVSLMEIDALLRQRIEELPEAQTRLFQCTVDMLHYFAGKQIRNVACLGGNIMTGSPISDMNPVLTAAGARLEVASIVEGKISQRTVHMGTGFFTGYRRNVIEPQEVLLGIHFQKTTPDQHVVAFKQARRRDDDIAIVNAAVNVRFEPKSNVVAEISMAFGGMAPTTVLAPRTSQLMVKQPLDHQLLERVAESLCGELPLAASAPGGMIAYRRALVVSLIFKAYLAISSKLSEAGIIAGDAIPPKERSGAELFHTPTLRSAQLFERVCSDQPVCDPIGRPEVHAAALKQATGEAIYTDDIPRMDGELYLGFVLSTKPRAKITKLDASAALALEGVHAFFSHKDLTVHENEVGPVFHDEHVFAAGEVHCYGQIVGAVAADNKALAQRASRLVRVEYEDLSPVIVTIEQAIEHGSYFPDYPRYVTKGNMAEAFAQAEHTYEGSCRMGGQEHFYLETHAAVAVPRDSDELELFCSTQHPSEVQKLVAHVTSLPAHRVVCRAKRLGGGFGGKESRGISVALPVALAAYRLRRPVRCMLDRDEDMLITGTRHPFLFKYKVAFSSDGLITACDIECYNNAGWSMDLSFSVLERAMYHFENCYHIPNVRVGGWVCKTNLPSNTAFRGFGGPQGMFAGEHIIRDVARIVGRDVLDVMRLNFYRTGDTTHYNQQLEHFPIERCLDDCLTQSRYHERRAEIAKFNRENRWRKRGVAVIPTKYGIAFGVMHLNQAGALLNVYGDGSVLLSHGGVEIGQGLNTKMIQCAARALGIPSELIHISETATDKVPNTSPTAASVGSDINGMAVLDACEKLNKRLAPIKEALPQATWQEWINKAYFDRVSLSATGFYAMPGIGYHPETNPNARTYSYYTNGVGISVVEIDCLTGDHQVLSTDIVMDIGSSINPAIDIGQIEGAFMQGYGLFTLEELMYSPQGMLYSRGPGMYKLPGFADIPGEFNVSLLTGAPNPRAVYSSKAVGEPPLFIGASAFFAIKEAIAAARQEHGLTGDFPLEAPSTSARIRMACQDKFTNLLEVPEAGSFTPWNIVP |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-96 | 2Fe-2S ferredoxin-type | ||||
Sequence: SVLVFFVNGKKVTDTNPDPECTLLTYLRDKLRLCGTKLGCAEGGCGACTVMISRMDRGQHKIRHLAVNACLTPVCAMHGCAVTTVEGI | ||||||
Domain | 236-425 | FAD-binding PCMH-type | ||||
Sequence: FSSERVTWYRPTTLQELLQLKAAHPAAKLVVGNTEVGVEVKFKHFLYPHLINPTLVAELQEVRESEESIYFGAAVSLMEIDALLRQRIEELPEAQTRLFQCTVDMLHYFAGKQIRNVACLGGNIMTGSPISDMNPVLTAAGARLEVASIVEGKISQRTVHMGTGFFTGYRRNVIEPQEVLLGIHFQKTTP |
Sequence similarities
Belongs to the xanthine dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,344
- Mass (Da)147,254
- Last updated1997-05-01 v1
- Checksum1DDB5BAC0E4C3175