1QQJ

CRYSTAL STRUCTURE OF MOUSE FUMARYLACETOACETATE HYDROLASE REFINED AT 1.55 ANGSTROM RESOLUTION

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qqja1	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	d1qqja2	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	d1qqjb1	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	d1qqjb2	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)
A	SCOP2B Superfamily	FAH N-terminal domain-like	8032393	3001866	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	FAH	8032394	3001446	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FAH	8032394	3001446	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FAH N-terminal domain-like	8032393	3001866	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)
A	FAA_hydrolase_N	e1qqjA1	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	e1qqjA2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: FAH (From Topology)	T: FAH	F: FAA_hydrolase	ECOD (1.6)
B	FAA_hydrolase_N	e1qqjB1	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	e1qqjB2	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)
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)
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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01557	Fumarylacetoacetate (FAA) hydrolase C-terminal (FAA_hydrolase)	Fumarylacetoacetate (FAA) hydrolase C-terminal	This entry consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydroly ...	This entry consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle [1]. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms [1]. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites [3]. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerises this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli Swiss:P77608 is involved in the phenylpropionic acid pathway of E. coli and catalyses the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor [5]. OHED hydratase encoded by hpcG in E. coli Swiss:P42270 is involved in the homoprotocatechuic acid (HPC) catabolism [6]. XylI in P. putida Swiss:P49155 is a 4-Oxalocrotonate decarboxylase [7].	Domain
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.