1Q0C

Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase from Brevibacterium fuscum. (Complex with 3,4-Dihydroxyphenylacetate)

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)
B	d1q0cb1	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Extradiol dioxygenases	Homoprotocatechuate 2,3-dioxygenase	(Brevibacterium fuscum ) [TaxId: 47914 ],	SCOPe (2.08)
C	d1q0cc1	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Extradiol dioxygenases	Homoprotocatechuate 2,3-dioxygenase	(Brevibacterium fuscum ) [TaxId: 47914 ],	SCOPe (2.08)
A	d1q0ca1	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Extradiol dioxygenases	Homoprotocatechuate 2,3-dioxygenase	(Brevibacterium fuscum ) [TaxId: 47914 ],	SCOPe (2.08)
D	d1q0cd1	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Extradiol dioxygenases	Homoprotocatechuate 2,3-dioxygenase	(Brevibacterium fuscum ) [TaxId: 47914 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044428	3000739	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044427	3000739	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044428	3000739	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044427	3000739	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044427	3000739	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044428	3000739	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044427	3000739	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8044428	3000739	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)
B	Glyoxalase	e1q0cB3	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	e1q0cB2	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_8	e1q0cB4	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_14	e1q0cB1	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_14	ECOD (1.6)
C	Glyoxalase	e1q0cC3	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)
C	Glyoxalase_11	e1q0cC2	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)
C	Glyoxalase_8	e1q0cC4	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)
C	Glyoxalase_14	e1q0cC1	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_14	ECOD (1.6)
A	Glyoxalase	e1q0cA3	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	e1q0cA2	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_8	e1q0cA4	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)
A	Glyoxalase_14	e1q0cA1	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_14	ECOD (1.6)
D	Glyoxalase	e1q0cD3	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)
D	Glyoxalase_11	e1q0cD2	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)
D	Glyoxalase_8	e1q0cD4	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)
D	Glyoxalase_14	e1q0cD1	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_14	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)
C	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)
A	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)
D	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, C, D	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, C, D	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, C, D	IPR050383	Glyoxalase I/Fosfomycin Resistance Protein Families	Family
A, B, C, D	IPR011981	3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn/Fe-type	Family
A, B, C, D	IPR029068	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Homologous Superfamily
A, B, C, D	IPR037523	Vicinal oxygen chelate (VOC) domain	Domain
A, B, C, D	IPR004360	Glyoxalase/fosfomycin resistance/dioxygenase domain	Domain
A, B, C, D	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.