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A0AAD9SY31 · A0AAD9SY31_9HELO

  • Protein
    xanthine dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Mo-molybdopterin (UniProtKB | Rhea| CHEBI:71302 )

Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 2 [2Fe-2S] clusters.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site53[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site58[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site61[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site86[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site125[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site128[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site169[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site171[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site382-389FAD (UniProtKB | ChEBI)
Binding site466FAD (UniProtKB | ChEBI)
Binding site476-480FAD (UniProtKB | ChEBI)
Binding site489FAD (UniProtKB | ChEBI)
Binding site553FAD (UniProtKB | ChEBI)
Binding site892Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Binding site923Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Binding site927substrate
Binding site1005substrate
Binding site1037Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Binding site1039substrate
Binding site1206Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Active site1395Proton acceptor

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular FunctionFAD binding
Molecular Functioniron ion binding
Molecular Functionmolybdopterin cofactor binding
Molecular Functionoxidoreductase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    xanthine dehydrogenase
  • EC number

Gene names

    • ORF names
      QTJ16_005193

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • R4
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Drepanopezizaceae > Diplocarpon

Accessions

  • Primary accession
    A0AAD9SY31

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain14-1042Fe-2S ferredoxin-type
Region241-288Disordered
Compositional bias247-279Polar residues
Domain354-543FAD-binding PCMH-type

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,464
  • Mass (Da)
    160,769
  • Last updated
    2024-05-29 v1
  • MD5 Checksum
    E0CCCD9C969106D96776887FD71B8215
MELTPEILSVFKESILTFYLNGMRVQLKDANPQWTLLDFIRSQHGLKGTKLGCGEGGCGACTVVLQVRGNHDEQKGRVKHMAVNACLFPLIGVEGKHVITVEGIGDVDNPHPLQERIAKLHGSQCGFCTPGIVMSLYALVRNSYDPVTKEYHLSASDIELEGHLDGNLCRCTGYKPILEAAKTFITEDLQGKIASSYISKAGVPSIDSKSEIIYRPESNLDRPLKNNGSCGRPGGCCRDGPKVSRKLSSSGELSKLSFDDSSETDSTSESATSCPGENETPINGAAYGKPMKSREIRGAVGDAVEGVKAASQLDIPPPEMKFGFPQIRFKLYSPVTELIFPPALRRHEKAPILFGTSTQFWLRPITLEQLLCIKDTYPSAKLVGGSSEVQVEIKFKNSLFPIAVYVSDIDELSKIAIPTDLYSMQELVIGANTTLTAVESVCRDLSPKLGYRGSVLEAIAKQLRYFAGRQIRNVASLAGNIATASPISDINPVLMACGATLTAQSISQGRLTLPMSAFFTGYRTTTLPPDAVITRIHIPIPASGTKELTKAYKQAKRKDDDIAVVTAAFRVRLDEAGAVSDISLVYGGMAPKTTEAKKTIKLMLGRKWDSQATLEGCMESLGGEFDLSFDVPGGMATYRKTLALSLFFRFWHETISDFGLGEVDRDLVHEIHRDISFGARDNYNPHEQRVVGKQVPHLSALKQNTGEAQYTDDIPKQDRELYGALVLSRRAHAKLVKVDWTPALGGGLALGYVDINSIPKESNLWGSVVKDEPFFADGEVFCHGQPIGLVYAETALQAQAAAKAVKIVYEDLPTILTIDEAIAANSFFRHGKMLKKGYALKHDMNGIWSKCDRVFEGVVRMGGQEHFYLETNAALVIPNKEDQSFEVWSSTQNTMEPQEFVAQVCGVPSSKVNVRVKRMGGAFGGKESRSVQLAVILAVAAKKTWRPVRCMLNRDEDMMTSGQRHPVQCRWKVGTATDGKLVALEADVYDNGGFSQDMSGAVMDRCCTHLENCYEIPHVLIRGHCCKTHTHSNTAFRGFGGPQAMFIAETYMSAVAEGLNIPIDELRRKNLYKTGDFTPFLQKIDQDWHIPMMLEQLRKEVEYDTRRAAIEKFNKEHRWRKRGMSMIPTKFGLSFATAVHLNQATASVKIYADGSILLHHGGTEMGQGLYTKMCQVAAQELNVPLDAIFTQDTTTYQSANASPTAASSGSDLNGMAVKNACDQLNERLQPFREKYGKDAPMKTLAHAAYLDRVSLTAAGYWKMPKIGYKWGSYDMTTVKPMYYYFTQGVAVSEVELDVLTGSHTVLRTDIKMDIGRSINPAIDYGQIEGAFVQGQGLFTMEESLWTRSGQLFTRGPGTYKIPGFSDIPQEFNVSFLQGVDWSHLRSIQSSKGVGEPPLFLGATVLFALREAVCSARRDNGVEEVLTLDSPATAERLRLAAGDAILKAGTVVPKEGERNFFVSVA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias247-279Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAUBYV010000007
EMBL· GenBank· DDBJ
KAK2625881.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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