The domain within your query sequence starts at position 717 and ends at position 1251; the E-value for the Ald_Xan_dh_C2 domain shown below is 1.3e-178.
IKHNSFLCPEKKLEQGNIEEAFENVDQVAEGTVHVGGQEHFYMETQRVLVIPKTEDKELD MYVSTQDPAHVQKTVSSTLNIPISRITCHVKRVGGGFGGKVGRPAVFGAIAAVGAVKTGH PIRLVLDREDDMLITGGRHPLFAKYKVGFMNSGRIKALDIECYINGGCTLDDSELVTEFL VLKLENAYKIRNLRLRGRACMTNLPSNTAFRGFGFPQGALVTESCITAVAAKCGLPPEKI REKNMYKTVDKTIYKQAFNPDPLIRCWNECLDKSSFHIRRTRVDEFNKKSYWKKRGIAIV PMKFSVGFAATSYHQAAALVHIYTDGSVLVAHGGNELGQGIHTKMLQVASRELKIPLSYL HICETSTTTVPNTIATAASVGADVNGRAVQNACQILLKRLEPVIKKNPEGTWRDWIEAAF EKRISLSATGYFRGYKAFMDWEKGEGDPFPYYVYGAACSEVEIDCLTGAHKKIRTDIVMD ACCSLNPAIDIGQIEGAFIQGMGLYTTEELLYSPEGVLYSRSPDKYKIPTVTDVP
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