The domain within your query sequence starts at position 709 and ends at position 1243; the E-value for the Ald_Xan_dh_C2 domain shown below is 1.1e-178.

LEHNSFLSPEKKIEQGNVDYAFKHVDQIVEGEIHVEGQEHFYMETQTILAIPQTEDKEMV
LHLGTQFPTHVQEFVSAALNVPRSRIACHMKRAGGAFGGKVTKPALLGAVCAVAANKTGR
PIRFILERSDDMLITAGRHPLLGKYKIGFMNNGEIRAADVEYYTNGGCTPDESELVIEFV
VLKSENTYHIPNFRCRGRACKTNLPSNTAFRGFGFPQATVVVEAYIAAVASKCNLLPEEV
REINMYKKTSKTAYKQTFNPEPLRRCWKECLEKSSFFARKKAAEEFNGNNYWKKRGLAVV
PMKFSVAVPIAFYNQAAALVHIFLDGSVLLTHGGCELGQGLHTKMIQVASRELNVPKSYV
HFSETSTTTVPNSAFTAGSMGADINGKAVQNACQILMDRLRPIIRKNPKGKWEEWIKMAF
EESISLSATGYFKGYQTNMDWKKEEGDPYPYYVYGAACSEVEVDCLTGAHKLLRTDIFVD
AAFSINPALDIGQVEGAFIQGMGFYTTEELKYSPKGVLYSRGPEDYKIPTITEIP

Ald_Xan_dh_C2

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