1DOC

THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1doca1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	p-Hydroxybenzoate hydroxylase, PHBH	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)
A	d1doca2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	PHBH-like	p-Hydroxybenzoate hydroxylase (PHBH)	(Pseudomonas aeruginosa ) [TaxId: 287 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Flavoreductase-like	8001363	3000055	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	FAD_binding_3_2nd	e1docA1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: FAD_binding_3_2nd	ECOD (1.6)
A	FAD_binding_3_1st	e1docA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.30.9.10	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01494	FAD binding domain (FAD_binding_3)	FAD binding domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	P-HYDROXYBENZOATE HYDROXYLASE	oxidoreductase activity catalytic activity monooxygenase activity 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity 4-hydroxybenzoate 3-monooxygenase [NADPH] 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, NAD(P)H as one donor, and incorporation of one atom of oxygen 4-hydroxybenzoate 3-monooxygenase activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding oxidoreductase activity catalytic activity monooxygenase activity 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity 4-hydroxybenzoate 3-monooxygenase [NADPH] 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, NAD(P)H as one donor, and incorporation of one atom of oxygen 4-hydroxybenzoate 3-monooxygenase activity FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	catabolic process benzene-containing compound metabolic process oxoacid metabolic process benzoate metabolic process cellular metabolic process carboxylic acid metabolic process organic acid metabolic process organic acid catabolic process organic cyclic compound catabolic process cellular catabolic process benzoate catabolic process organic cyclic compound metabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process catabolic process benzene-containing compound metabolic process oxoacid metabolic process benzoate metabolic process cellular metabolic process carboxylic acid metabolic process organic acid metabolic process organic acid catabolic process organic cyclic compound catabolic process cellular catabolic process benzoate catabolic process organic cyclic compound metabolic process organic substance metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process metabolic process small molecule metabolic process cellular process benzoate catabolic process via hydroxylation monocarboxylic acid metabolic process small molecule catabolic process organic substance catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR012733	4-hydroxybenzoate 3-monooxygenase	Family
A	IPR002938	FAD-binding domain	Domain
A	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	4-hydroxybenzoate 3-monooxygenase M-CSA #131	4-hydroxybenzoate 3-monooxygenase is a flavoprotein that catalyses the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). 3,4DOHB subsequently enters the beta-ketioadipate pathway of aromatic degradation, using molecular oxygen and NADPH. The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.	Defined by 5 residues: HIS:A-72TYR:A-201PRO:A-293LYS:A-297TYR:A-385 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.