Fumarylacetoacetase, N-terminal (IPR015377)

Short name: Fumarylacetoacetase_N

Overlapping homologous superfamilies

Domain relationships



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 [PMID: 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 [PMID: 16602095, PMID: 9101289]. The enzyme mechanism involves a catalytic metal ion, a Glu/His catalytic dyad, and a charged oxyanion hole [PMID: 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 [PMID: 10508789].

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

GO terms

Biological Process

GO:0009072 aromatic amino acid family metabolic process

Molecular Function

GO:0004334 fumarylacetoacetase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.