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Quercetin 2,3-dioxygenase in complex with the inhibitor diethyldithiocarbamate External Resource: Annotation Chains Domain Info Class Fold Superfamily Family Domain Species Provenance Source (Version) A d1gqga_ All beta proteins Double-stranded beta-helix RmlC-like cupins Quercetin 2,3-dioxygenase-like Quercetin 2,3-dioxygenase Aspergillus japonicus ) [TaxId: 34381 ], SCOPe (2.08) B d1gqgb_ All beta proteins Double-stranded beta-helix RmlC-like cupins Quercetin 2,3-dioxygenase-like Quercetin 2,3-dioxygenase Aspergillus japonicus ) [TaxId: 34381 ], SCOPe (2.08) C d1gqgc_ All beta proteins Double-stranded beta-helix RmlC-like cupins Quercetin 2,3-dioxygenase-like Quercetin 2,3-dioxygenase Aspergillus japonicus ) [TaxId: 34381 ], SCOPe (2.08) D d1gqgd_ All beta proteins Double-stranded beta-helix RmlC-like cupins Quercetin 2,3-dioxygenase-like Quercetin 2,3-dioxygenase Aspergillus japonicus ) [TaxId: 34381 ], SCOPe (2.08)
Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2B Superfamily RmlC-like cupins 8042344 3001825 SCOP2B (2022-06-29) B SCOP2B Superfamily RmlC-like cupins 8042344 3001825 SCOP2B (2022-06-29) C SCOP2B Superfamily RmlC-like cupins 8042344 3001825 SCOP2B (2022-06-29) D SCOP2B Superfamily RmlC-like cupins 8042344 3001825 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A EutQ_1 e1gqgA3 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: EutQ_1 ECOD (1.6) A Cupin_2 e1gqgA2 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: Cupin_2 ECOD (1.6) B EutQ_1 e1gqgB3 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: EutQ_1 ECOD (1.6) B Cupin_2 e1gqgB2 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: Cupin_2 ECOD (1.6) C EutQ_1 e1gqgC3 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: EutQ_1 ECOD (1.6) C Cupin_2 e1gqgC2 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: Cupin_2 ECOD (1.6) D EutQ_1 e1gqgD3 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: EutQ_1 ECOD (1.6) D Cupin_2 e1gqgD2 A: beta sandwiches X: jelly-roll H: Double-stranded beta-helix (From Topology) T: Double-stranded beta-helix F: Cupin_2 ECOD (1.6)
Chains Polymer Molecular Function Biological Process Cellular Component QUERCETIN 2,3-DIOXYGENASE - -
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage Chains Enzyme Name Description Catalytic Residues quercetin 2,3-dioxygenase
M-CSA #743 Quercetin 2,3-dioxygenase is a copper-dependent enzyme that catalyses the reaction of dioxygen with quercin (3,5,7,3',4'-pentahydroxy flavone). Dioxygenases are enzymes that catalyses the incorporation of both atoms of molecular oxygen into organic substrates, most notably during the degradation of aromatic compounds. They typically use a metal ion to circumvent the spin barrier that prevents the direct reaction of the triplet ground state of dioxygen with singlet-state organic compounds. In most of the well-studied dioxygenases, the metal used is iron; quercetin 2,3-dioxygenase is the only known member of this family to use copper.
