2V27

Structure of the cold active phenylalanine hydroxylase from Colwellia psychrerythraea 34H

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Biopterin_H	e2v27A1	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)
B	Biopterin_H	e2v27B1	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)
A	1.10.800.10	Mainly Alpha	Orthogonal Bundle	Phenylalanine Hydroxylase	Aromatic amino acid hydroxylase	CATH (4.3.0)
B	1.10.800.10	Mainly Alpha	Orthogonal Bundle	Phenylalanine Hydroxylase	Aromatic amino acid hydroxylase	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PHENYLALANINE HYDROXYLASE	oxidoreductase activity 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 phenylalanine 4-monooxygenase activity catalytic activity cation binding transition metal ion binding iron ion 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	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036951	Aromatic amino acid hydroxylase superfamily	Homologous Superfamily
A, B	IPR005960	Phenylalanine-4-hydroxylase, monomeric form	Family
A, B	IPR019774	Aromatic amino acid hydroxylase, C-terminal	Domain
A, B	IPR001273	Aromatic amino acid hydroxylase	Family
A, B	IPR018301	Aromatic amino acid hydroxylase, iron/copper binding site	Binding Site
A, B	IPR036329	Aromatic amino acid monoxygenase, C-terminal domain superfamily	Homologous Superfamily

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.