5FII

Structure of a human aspartate kinase, chorismate mutase and TyrA domain.

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ACT_1	e5fiiA1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_1	ECOD (1.6)
C	ACT_1	e5fiiC1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_1	ECOD (1.6)
D	ACT_1	e5fiiD1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_1	ECOD (1.6)
B	ACT_1	e5fiiB1	A: a+b two layers	X: Alpha-beta plaits	H: ACT-like (From Topology)	T: ACT-like	F: ACT_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
C	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
D	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)
B	3.30.70.260	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	ACT domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01842	ACT domain (ACT)	ACT domain	This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulati ...	This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	PHENYLALANINE-4-HYDROXYLASE	cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding 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	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 amino acid biosynthetic process biosynthetic 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 proteinogenic amino acid biosynthetic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid biosynthetic process tyrosine biosynthetic process alpha-amino acid biosynthetic process organic hydroxy compound metabolic process catechol-containing compound metabolic process amine metabolic process biogenic amine biosynthetic process catecholamine metabolic process amine biosynthetic process phenol-containing compound metabolic process organic hydroxy compound biosynthetic process catecholamine biosynthetic process phenol-containing compound biosynthetic process catechol-containing compound biosynthetic process biogenic amine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR019773	Tyrosine 3-monooxygenase-like	Family
A, B, C, D	IPR005961	Phenylalanine-4-hydroxylase, tetrameric form	Family
A, B, C, D	IPR019774	Aromatic amino acid hydroxylase, C-terminal	Domain
A, B, C, D	IPR045865	ACT-like domain	Homologous Superfamily
A, B, C, D	IPR002912	ACT domain	Domain
A, B, C, D	IPR041912	Eukaryotic phenylalanine-4-hydroxylase, catalytic domain	Domain
A, B, C, D	IPR036329	Aromatic amino acid monoxygenase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR036951	Aromatic amino acid hydroxylase superfamily	Homologous Superfamily
A, B, C, D	IPR001273	Aromatic amino acid hydroxylase	Family
A, B, C, D	IPR018301	Aromatic amino acid hydroxylase, iron/copper binding site	Binding Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P00439	phenylketonuria Classical phenylketonuria pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia atypical teratoid rhabdoid tumor glioblastoma interstitial cystitis lung carcinoma medulloblastoma pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma schizophrenia bipolar disorder drug-induced liver injury hyperphenylalaninemia due to tetrahydrobiopterin deficiency phenylketonuria Classical phenylketonuria pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia atypical teratoid rhabdoid tumor glioblastoma interstitial cystitis lung carcinoma medulloblastoma pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma schizophrenia bipolar disorder drug-induced liver injury hyperphenylalaninemia due to tetrahydrobiopterin deficiency inborn errors of metabolism large cell medulloblastoma malignant ependymoma nephrosclerosis pancreatic intraductal papillary-mucinous neoplasm primitive neuroectodermal tumor Sjogren syndrome classic phenylketonuria intellectual disability lung cancer malignant glioma

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.