Annotations: 5JK8

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	ACT_1	e5jk8B1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_1	ECOD (1.6)
B	Biopterin_H	e5jk8B2	A: a+b complex topology	X: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains (From Topology)	H: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains (From Topology)	T: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains	F: Biopterin_H	ECOD (1.6)
A	ACT_1	e5jk8A2	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_1	ECOD (1.6)
A	Biopterin_H	e5jk8A1	A: a+b complex topology	X: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains (From Topology)	H: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains (From Topology)	T: Aromatic aminoacid monoxygenases, catalytic and oligomerization domains	F: Biopterin_H	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.800.10	Mainly Alpha	Orthogonal Bundle	Phenylalanine Hydroxylase	Aromatic amino acid hydroxylase	CATH (4.3.0)
A	1.10.800.10	Mainly Alpha	Orthogonal Bundle	Phenylalanine Hydroxylase	Aromatic amino acid hydroxylase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00351	Biopterin-dependent aromatic amino acid hydroxylase (Biopterin_H)	Biopterin-dependent aromatic amino acid hydroxylase	This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Phenylalanine-4-hydroxylase	oxidoreductase activity monooxygenase activity tryptophan 5-monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding organic cyclic compound binding oxidoreductase activity monooxygenase activity tryptophan 5-monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen catalytic activity cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding organic cyclic compound binding tetrahydrobiopterin binding phenylalanine 4-monooxygenase activity prephenate dehydratase activity hydro-lyase activity lyase activity carbon-oxygen lyase activity identical protein binding protein 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 organic acid biosynthetic process carboxylic acid biosynthetic process tyrosine metabolic process aromatic amino acid family biosynthetic process small molecule biosynthetic process L-amino acid biosynthetic process aromatic amino acid family biosynthetic process, prephenate pathway amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid biosynthetic process tyrosine biosynthetic process alpha-amino acid biosynthetic process L-phenylalanine biosynthetic process reproductive process asexual reproduction	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR019773	Tyrosine 3-monooxygenase-like	Family
A, B	IPR019774	Aromatic amino acid hydroxylase, C-terminal	Domain
A, B	IPR045865	ACT-like domain	Homologous Superfamily
A, B	IPR002912	ACT domain	Domain
A, B	IPR041912	Eukaryotic phenylalanine-4-hydroxylase, catalytic domain	Domain
A, B	IPR036329	Aromatic amino acid monoxygenase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR036951	Aromatic amino acid hydroxylase superfamily	Homologous Superfamily
A, B	IPR018528	Prephenate dehydratase, conserved site	Conserved Site
A, B	IPR001273	Aromatic amino acid hydroxylase	Family
A, B	IPR018301	Aromatic amino acid hydroxylase, iron/copper binding site	Binding Site

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.