2DKH

Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni, in complex with the substrate

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
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	PRK08294	e2dkhA2	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: PRK08294	ECOD (1.6)
A	Phe_hydrox_dim	e2dkhA4	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Phe_hydrox_dim	ECOD (1.6)
A	FAD_binding_3_3rd	e2dkhA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_3rd	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)
A	3.40.30.20	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Phenol hydroxylase, C-terminal dimerisation domain	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
A	PF07976	Phenol hydroxylase, C-terminal dimerisation domain (Phe_hydrox_dim)	Phenol hydroxylase, C-terminal dimerisation domain	Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerisation i ...	Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerisation interface. The domain adopts a thioredoxin-like fold [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	3-hydroxybenzoate hydroxylase	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity monooxygenase activity 3-hydroxybenzoate 4-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, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity FAD binding flavin adenine dinucleotide binding nucleoside phosphate binding identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity monooxygenase activity 3-hydroxybenzoate 4-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, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity FAD binding flavin adenine dinucleotide binding nucleoside phosphate binding ion binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR002938	FAD-binding domain	Domain
A	IPR038220	Phenol hydroxylase, C-terminal TRX-fold domain superfamily	Homologous Superfamily
A	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR012941	Phenol hydroxylase-like, C-terminal dimerisation domain	Domain
A	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A	IPR050641	Rifampicin monooxygenase-like	Family

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.