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.
QNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLFTGPALSKHQHVFDETTLNNFMGLG QAAWKEARASLQNLLSASQARLRDDKELRQRAFTSQASATMHLP
FAA_hydrolase_N |
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| PFAM accession number: | PF09298 |
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| Interpro abstract (IPR015377): | Fumarylacetoacetase ( EC 3.7.1.2 ; 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