Annotations: 1BOU

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1boua_	All alpha proteins	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	(Sphingomonas paucimobilis ) [TaxId: 13689 ],	SCOPe (2.08)
C	d1bouc_	All alpha proteins	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	(Sphingomonas paucimobilis ) [TaxId: 13689 ],	SCOPe (2.08)
B	d1boub_	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	LigB-like	LigB-like	LigB subunit of an aromatic-ring-opening dioxygenase LigAB	(Sphingomonas paucimobilis ) [TaxId: 13689 ],	SCOPe (2.08)
D	d1boud_	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	LigB-like	LigB-like	LigB subunit of an aromatic-ring-opening dioxygenase LigAB	(Sphingomonas paucimobilis ) [TaxId: 13689 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	8025700	4001114	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	8038079	3000805	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	LigA subunit of an aromatic-ring-opening dioxygenase LigAB	8038079	3000805	SCOP2B (2022-06-29)
B	SCOP2 Family	LigB-like	8019828	4000592	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	LigB-like	8032208	3000690	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	LigB-like	8032208	3000690	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	LigA	e1bouA1	A: alpha arrays	X: LigA subunit of an aromatic-ring-opening dioxygenase LigAB (From Topology)	H: LigA subunit of an aromatic-ring-opening dioxygenase LigAB (From Topology)	T: LigA subunit of an aromatic-ring-opening dioxygenase LigAB	F: LigA	ECOD (1.6)
C	LigA	e1bouC1	A: alpha arrays	X: LigA subunit of an aromatic-ring-opening dioxygenase LigAB (From Topology)	H: LigA subunit of an aromatic-ring-opening dioxygenase LigAB (From Topology)	T: LigA subunit of an aromatic-ring-opening dioxygenase LigAB	F: LigA	ECOD (1.6)
B	LigB	e1bouB1	A: a/b three-layered sandwiches	X: LigB-like (From Topology)	H: LigB-like (From Topology)	T: LigB-like	F: LigB	ECOD (1.6)
D	LigB	e1bouD1	A: a/b three-layered sandwiches	X: LigB-like (From Topology)	H: LigB-like (From Topology)	T: LigB-like	F: LigB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.700.10	Mainly Alpha	Orthogonal Bundle	Protocatechuate 4,5-dioxygenase	Chain A	CATH (4.3.0)
C	1.10.700.10	Mainly Alpha	Orthogonal Bundle	Protocatechuate 4,5-dioxygenase	Chain A	CATH (4.3.0)
B	3.40.830.10	Alpha Beta	3-Layer(aba) Sandwich	Protocatechuate 4,5-dioxygenase	Chain B	CATH (4.3.0)
D	3.40.830.10	Alpha Beta	3-Layer(aba) Sandwich	Protocatechuate 4,5-dioxygenase	Chain B	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF07746	Aromatic-ring-opening dioxygenase LigAB, LigA subunit (LigA)	Aromatic-ring-opening dioxygenase LigAB, LigA subunit	-	Family
B, D	PF02900	Catalytic LigB subunit of aromatic ring-opening dioxygenase (LigB)	Catalytic LigB subunit of aromatic ring-opening dioxygenase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	4,5-DIOXYGENASE ALPHA CHAIN	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 protocatechuate 4,5-dioxygenase activity dioxygenase activity	-	-
B, D	4,5-DIOXYGENASE BETA CHAIN	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 protocatechuate 4,5-dioxygenase activity dioxygenase activity cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR011986	Extradiol ring-cleavage dioxygenase LigAB, LigA subunit	Domain
A, C	IPR014159	Protocatechuate 4,5-dioxygenase, alpha subunit	Family
A, C	IPR036622	Dioxygenase LigAB, LigA subunit superfamily	Homologous Superfamily
B, D	IPR034937	Protocatechuate 4,5-dioxygenase beta chain	Family
B, D	IPR004183	Extradiol ring-cleavage dioxygenase, class III enzyme, subunit B	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
B	protocatechuate 4,5-dioxygenase M-CSA #672	The LigAB enzyme from Sphingomonas paucimobilis SYK-6 is a protocatechuate 4,5-dioxygenase, catalyses the ring-opening of protocatechuate (PCA) by oxidation to cleave the C4-C5 bond adjacent to the vicinal hydroxyl group. It belongs to the family of class III extradiol-type catecholic dioxygenase which is characterised by a ferrous iron in the active site. It has been identified as a key enzyme in the lignin-degradation pathway of Sphingomonas paucimobilis SYK-6.	Defined by 4 residues: HIS:B-12HIS:B-61HIS:B-195GLU:B-242 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.13.11.8 (PDB Primary Data) Search M-CSA Motif + EC 1.13.11.8

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.