The domain within your query sequence starts at position 15 and ends at position 118; the E-value for the FAA_hydrolase_N domain shown below is 1.7e-36.



PFAM accession number:PF09298
Interpro abstract (IPR015377):

Fumarylacetoacetase ( EC ; also known as fumarylacetoacetate hydrolase or FAH) catalyses the hydrolytic cleavage of a carbon-carbon bond in fumarylacetoacetate to yield fumarate and acetoacetate as the final step in phenylalanine and tyrosine degradation [ (PUBMED:11154690) ]. This is an essential metabolic function in humans, the lack of FAH causing type I tyrosinaemia, which is associated with liver and kidney abnormalities and neurological disorders [ (PUBMED:16602095) (PUBMED:9101289) ]. The enzyme mechanism involves a catalytic metal ion, a Glu/His catalytic dyad, and a charged oxyanion hole [ (PUBMED:10508789) ]. FAH folds into two domains: an N-terminal domain SH3-like beta-barrel, and a C-terminal with an unusual fold consisting of three layers of beta-sheet structures [ (PUBMED:10508789) ].

This entry represents the N-terminal domain of fumarylacetoacetase. This domain adopts a structure consisting of an SH3-like barrel [ (PUBMED:11154690) ].

GO process:aromatic amino acid family metabolic process (GO:0009072)
GO function:fumarylacetoacetase activity (GO:0004334)

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