The domain within your query sequence starts at position 123 and ends at position 413; the E-value for the FAA_hydrolase domain shown below is 1e-58.

DYTDFYSSRQHATNVGIMFRGKENALLPNWLHLPVGYHGRASSIVVSGTPIRRPMGQMRP
DNSKPPVYGACRLLDMELEMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQW
EYVPLGPFLGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLSVS
LKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGSDPESFGSM
LELSWKGTKAIDVEQGQTRTFLLDGDEVIITGHCQGDGYRVGFGQCAGKVL

FAA_hydrolase

 FAA_hydrolase
PFAM accession number:PF01557
Interpro abstract (IPR011234):

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:9101289) (PUBMED:16602095) ]. 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 C-terminal domain of fumarylacetoacetase, as well as other domains that share a homologous alpha/beta structure, including:

  • 5-carboxymethyl-2-hydroxymuconate delta-isomerase (CHM isomerase; EC 5.3.3.10 ), which catalyses the conversion of 5-carboxymethyl-2-hydroxymuconate to 5-carboxy-2-oxohept-3-enedioate [ (PUBMED:2194841) ].
  • 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase (OPET decarboxylase; EC 4.1.1.68 ), which catalyses the conversion of 5-oxopent-3-ene-1,2,5-tricarboxylate to 2-oxohept-3-enedioate and carbon dioxide.
  • Bifunctional enzyme HpcE (OPET decarboxylase EC 4.1.1.68 /HHDD isomerase EC 5.3.3.10 ), which is a duplication consisting of a tandem repeat of two FAH C-terminal-like domains. This enzyme is responsible for the degradation of 4-hydroxyphenylacetate, a product of tyrosine and phenylalanine metabolism also released by lignin catabolism [ (PUBMED:11863436) ].
  • 2-keto-4-pentenoate hydratase MhpD ( EC 4.2.1.80 ; also known as 2-oxopent-4-enoate hydratase), which converts 4-hydroxy-2-oxopentanoate to 2-oxopent-4-enoate [ (PUBMED:10537203) ].
  • 4-oxalocrotonate decarboxylase (4-OD; EC 4.1.1.77 ), which catalyses the conversion of 4-oxalocrotonate to 2-oxopent-4-enoate and carbon dioxide [ (PUBMED:10651637) ].
  • 2-oxo-hepta-3-ene-1,7-dioic acid hydratase, which hydrates the double bond of 2-oxo-hepta-3-ene-1,7-dioic acid to form 4-hydroxy-2-oxo-heptane-1,7-dioic acid in the catabolism of 4-hydroxyphenylacetic acid.
GO function:catalytic activity (GO:0003824)

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