SUPERFAMILY 1.75 HMM library and genome assignments server

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FAH superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a+b) [ 53931] (376)
Fold:   FAH [ 56528]
Superfamily:   FAH [ 56529]
Families:   FAH [ 56530] (6)

Superfamily statistics
Genomes (2,312) Uniprot 2017_06 genome PDB chains (SCOP 1.75)
Domains 8,182 52,609 9
Proteins 8,083 52,247 8

Functional annotation
General category Metabolism
Detailed category Other enzymes

Function annotation of SCOP domain superfamilies

Gene Ontology (high-quality)

(show details)
GO termFDR (singleton)FDR (all)SDFO levelAnnotation (direct or inherited)
Molecular Function (MF)hydrolase activity0.0084190.003166Least InformativeInherited
Molecular Function (MF)lyase activity0.00000019940.000001357Moderately InformativeDirect
Molecular Function (MF)carbon-carbon lyase activity0.021180.03InformativeInherited
Molecular Function (MF)carboxy-lyase activity0.00000000013820.00000004812Highly InformativeDirect

Document: GO annotation of SCOP domains

Gene Ontology (high-coverage)

(show details)
GO term FDR (all) SDFO level Annotation (direct or inherited)
Biological Process (BP) single-organism metabolic process 0.8633 Least Informative Inherited
Biological Process (BP) single-organism catabolic process 0.002926 Moderately Informative Inherited
Molecular Function (MF) hydrolase activity 0.003166 Least Informative Inherited
Molecular Function (MF) lyase activity 0.000001357 Moderately Informative Direct
Molecular Function (MF) carbon-carbon lyase activity 0.03 Informative Inherited
Molecular Function (MF) carboxy-lyase activity 0.00000004812 Highly Informative Direct

Document: GO annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Lyases0Least InformativeDirect
Enzyme Commission (EC)Hydro-lyases0Moderately InformativeDirect
Enzyme Commission (EC)Carboxy-lyases0.00009809Moderately InformativeDirect
Enzyme Commission (EC)Carbon-nitrogen lyases0.00109InformativeInherited
Enzyme Commission (EC)Lyases acting on amides, amidines, etc0.00000000001057Highly InformativeDirect
Enzyme Commission (EC)In ketonic substances1Highly InformativeInherited

Document: EC annotation of SCOP domains

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processAromatic hydrocarbons catabolism0InformativeDirect
Biological processPhenylalanine catabolism0.000000000000004737Highly InformativeDirect
Biological processNucleotide metabolism0.000000009735Highly InformativeDirect
DomainTransit peptide0.0008675Moderately InformativeDirect
Molecular functionMetal-binding0.000000000000126Least InformativeDirect
Molecular functionMagnesium0.00000005195Least InformativeDirect
Molecular functionCalcium0Moderately InformativeDirect
Post-translational modificationHydrolase0.00006342Least InformativeDirect
Post-translational modificationLyase0Moderately InformativeDirect
Post-translational modificationAcetylation0.000001002Least InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR011234 SSF56529 Protein matches

Fumarylacetoacetase (; 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 [PubMed11154690]. 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 [PubMed9101289, PubMed16602095]. The enzyme mechanism involves a catalytic metal ion, a Glu/His catalytic dyad, and a charged oxyanion hole [PubMed10508789]. 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 [PubMed10508789].

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), which catalyses the conversion of 5-carboxymethyl-2-hydroxymuconate to 5-carboxy-2-oxohept-3-enedioate [PubMed2194841].
  • 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase (OPET decarboxylase), 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 /HHDD isomerase ), 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 [PubMed11863436].
  • 2-keto-4-pentenoate hydratase MhpD (; also known as 2-oxopent-4-enoate hydratase), which converts 4-hydroxy-2-oxopentanoate to 2-oxopent-4-enoate [PubMed10537203].
  • 4-oxalocrotonate decarboxylase (4-OD), which catalyses the conversion of 4-oxalocrotonate to 2-oxopent-4-enoate and carbon dioxide [PubMed10651637].
  • 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.

InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Gene Ontology (high-quality) · Gene Ontology (high-coverage) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.

Alignments of sequences to 7 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.

Browse and view proteins in genomes which have different domain combinations including a FAH domain.

Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.

Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 7 hidden Markov models representing the FAH superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Gene Ontology (high-quality) · Gene Ontology (high-coverage) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) · Internal database links ]