Annotations: 1QCN

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1qcnb1	All beta proteins	SH3-like barrel	Fumarylacetoacetate hydrolase, FAH, N-terminal domain	Fumarylacetoacetate hydrolase, FAH, N-terminal domain	Fumarylacetoacetate hydrolase, FAH, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1qcnb2	Alpha and beta proteins (a+b)	FAH	FAH	FAH	Fumarylacetoacetate hydrolase, FAH, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1qcnb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d1qcna1	All beta proteins	SH3-like barrel	Fumarylacetoacetate hydrolase, FAH, N-terminal domain	Fumarylacetoacetate hydrolase, FAH, N-terminal domain	Fumarylacetoacetate hydrolase, FAH, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d1qcna2	Alpha and beta proteins (a+b)	FAH	FAH	FAH	Fumarylacetoacetate hydrolase, FAH, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	FAH	8032394	3001446	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FAH N-terminal domain-like	8032393	3001866	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	FAH N-terminal domain-like	8032393	3001866	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	FAH	8032394	3001446	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	FAA_hydrolase_N	e1qcnB1	A: beta barrels	X: SH3	H: Fumarylacetoacetate hydrolase, FAH, N-terminal domain (From Topology)	T: Fumarylacetoacetate hydrolase, FAH, N-terminal domain	F: FAA_hydrolase_N	ECOD (1.6)
B	FAA_hydrolase	e1qcnB2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: FAH (From Topology)	T: FAH	F: FAA_hydrolase	ECOD (1.6)
A	FAA_hydrolase_N	e1qcnA1	A: beta barrels	X: SH3	H: Fumarylacetoacetate hydrolase, FAH, N-terminal domain (From Topology)	T: Fumarylacetoacetate hydrolase, FAH, N-terminal domain	F: FAA_hydrolase_N	ECOD (1.6)
A	FAA_hydrolase	e1qcnA2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: FAH (From Topology)	T: FAH	F: FAA_hydrolase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	2.30.30.230	Mainly Beta	Roll	SH3 type barrels.	Fumarylacetoacetase, N-terminal domain	CATH (4.3.0)
B	3.90.850.10	Alpha Beta	Alpha-Beta Complex	Fumarylacetoacetate hydrolase	domain 2	CATH (4.3.0)
A	2.30.30.230	Mainly Beta	Roll	SH3 type barrels.	Fumarylacetoacetase, N-terminal domain	CATH (4.3.0)
A	3.90.850.10	Alpha Beta	Alpha-Beta Complex	Fumarylacetoacetate hydrolase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01557	Fumarylacetoacetate (FAA) hydrolase family (FAA_hydrolase)	Fumarylacetoacetate (FAA) hydrolase family	-	Family
A, B	PF09298	Fumarylacetoacetase N-terminal (FAA_hydrolase_N)	Fumarylacetoacetase N-terminal	The N-terminal domain of fumarylacetoacetate hydrolase is functionally uncharacterised, and adopts a structure consisting of an SH3-like barrel [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	FUMARYLACETOACETATE HYDROLASE	hydrolase activity, acting on acid carbon-carbon bonds fumarylacetoacetase activity hydrolase activity hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances catalytic activity cation binding ion binding binding metal ion binding small molecule binding	catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine catabolic process aromatic amino acid metabolic process catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine catabolic process aromatic amino acid metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process L-phenylalanine metabolic process proteinogenic amino acid metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process tyrosine metabolic process tyrosine catabolic process glutamine family amino acid catabolic process arginine catabolic process glutamine family amino acid metabolic process arginine metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036663	Fumarylacetoacetase-like, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR036462	Fumarylacetoacetase, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR005959	Fumarylacetoacetase	Family
A, B	IPR011234	Fumarylacetoacetase-like, C-terminal	Domain
A, B	IPR015377	Fumarylacetoacetase, N-terminal	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.