1F1U | pdb_00001f1u

CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM ARTHROBACTER GLOBIFORMIS (NATIVE, LOW TEMPERATURE)

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1f1ua1	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Extradiol dioxygenases	Homoprotocatechuate 2,3-dioxygenase	(Arthrobacter globiformis ) [TaxId: 1665 ],	SCOPe (2.08)
B	d1f1ub1	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Extradiol dioxygenases	Homoprotocatechuate 2,3-dioxygenase	(Arthrobacter globiformis ) [TaxId: 1665 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Extradiol dioxygenases	8032047	4001093	SCOP2 (2022-06-29)
A	SCOP2 Family	Extradiol dioxygenases	8032048	4001093	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044425	3000739	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044426	3000739	SCOP2 (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	Glyoxalase	e1f1uA3	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase	ECOD (1.6)
A	Glyoxalase_11	e1f1uA2	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_11	ECOD (1.6)
A	Glyoxalase_6	e1f1uA1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_6	ECOD (1.6)
A	Glyoxalase_8	e1f1uA4	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_8	ECOD (1.6)
B	Glyoxalase	e1f1uB3	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase	ECOD (1.6)
B	Glyoxalase_11	e1f1uB2	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_11	ECOD (1.6)
B	Glyoxalase_6	e1f1uB1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_6	ECOD (1.6)
B	Glyoxalase_8	e1f1uB4	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_8	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)
B	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00903	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (Glyoxalase)	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	HOMOPROTOCATECHUATE 2,3-DIOXYGENASE	oxidoreductase activity 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	IPR050383	Glyoxalase I/Fosfomycin Resistance Protein Families	Family
A, B	IPR037523	Vicinal oxygen chelate (VOC), core domain	Domain
A, B	IPR011981	3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn/Fe-type	Family
A, B	IPR029068	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Homologous Superfamily
A, B	IPR004360	Glyoxalase/fosfomycin resistance/dioxygenase domain	Domain
A, B	IPR044904	3,4-dihydroxyphenylacetate 2,3-dioxygenase, C-terminal domain superfamily	Homologous Superfamily

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.