The domain within your query sequence starts at position 708 and ends at position 1241; the E-value for the Ald_Xan_dh_C2 domain shown below is 8.7e-183.

QYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDI
YVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRP
IRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYAL
LKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVR
ELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIP
MKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIH
LDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFV
QSISLSATGYFRGYQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDG
SFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIP

Ald_Xan_dh_C2

• PFAM accession number: PF02738
• Interpro abstract (IPR008274):

  Aldehyde oxidase ( EC 1.2.3.1 ) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase ( EC 1.1.1.204 ) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase ( EC 1.1.3.22 ) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.

• GO process: oxidation-reduction process (GO:0055114)
• GO function: oxidoreductase activity (GO:0016491)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ald_Xan_dh_C2