The domain within your query sequence starts at position 153 and ends at position 292; the E-value for the Uricase domain shown below is 5.6e-38.
IHSGIKDLKVLKTTQSGFEGFLKDQFTTLPEVKDRCFATQVYCKWRYQRRDVDFEAIWGA
VRDIVLQKFAGPYDKGEYSPSVQKTLYDIQVLSLSQLPEIEDMEISLPNIHYFNIDMSKM
GLINKEEVLLPLDNPYGKIT
Uricase |
|
---|
PFAM accession number: | PF01014 |
---|
Interpro abstract (IPR002042): |
Uricase ( EC 1.7.3.3 ) (urate oxidase) [ (PUBMED:3182808) ] is the peroxisomal enzyme responsible for the degradation of urate into allantoin: Urate + O 2 + H 2 O = 5-hydroxyisourate + H 2 O 2 Some species, like primates and birds, have lost the gene for uricase and are therefore unable to degrade urate [ (PUBMED:2594778) ]. Uricase is a protein of 300 to 400 amino acids, its sequence is well conserved. It is mainly localised in the liver, where it forms a large electron-dense paracrystalline core in many peroxisomes [ (PUBMED:2338140) ]. The enzyme exists as a tetramer of identical subunits, each containing a possible type 2 copper-binding site [ (PUBMED:2594778) ]. In legumes, 2 forms of uricase are found: in the roots, the tetrameric form; and, in the uninfected cells of root nodules, a monomeric form, which plays an important role in nitrogen-fixation [ (PUBMED:16593585) ].
|
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Uricase