Annotations: 1JUH

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1juha_	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	d1juhb_	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	d1juhc_	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	d1juhd_	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)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

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)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EutQ_1	e1juhA2	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	e1juhA3	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	e1juhB3	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	e1juhB2	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	e1juhC3	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	e1juhC2	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	e1juhD3	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	e1juhD2	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: Cupin_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)
B	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)
C	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)
D	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	quercetin 2,3-dioxygenase	quercetin 2,3-dioxygenase activity oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen oxidoreductase activity oxidoreductase activity, acting on single donors with incorporation of molecular oxygen catalytic activity dioxygenase activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR011051	RmlC-like cupin domain superfamily	Homologous Superfamily
A, B, C, D	IPR014710	RmlC-like jelly roll fold	Homologous Superfamily

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.