1CB8

CHONDROITINASE AC LYASE FROM FLAVOBACTERIUM HEPARINUM

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1cb8a1	All alpha proteins	alpha/alpha toroid	Chondroitin AC/alginate lyase	Hyaluronate lyase-like catalytic, N-terminal domain	Chondroitinase AC	(Pedobacter heparinus ) [TaxId: 984 ],	SCOPe (2.08)
A	d1cb8a2	All beta proteins	Hyaluronate lyase-like, C-terminal domain	Hyaluronate lyase-like, C-terminal domain	Hyaluronate lyase-like, C-terminal domain	Chondroitinase AC	(Pedobacter heparinus ) [TaxId: 984 ],	SCOPe (2.08)
A	d1cb8a3	All beta proteins	Supersandwich	Galactose mutarotase-like	Hyaluronate lyase-like, central domain	Chondroitinase AC	(Pedobacter heparinus ) [TaxId: 984 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Hyaluronate lyase-like central domain	8029157	4001655	SCOP2 (2022-06-29)
A	SCOP2 Family	Hyaluronate lyase-like C-terminal domain	8028877	4002575	SCOP2 (2022-06-29)
A	SCOP2 Family	Hyaluronate lyase-like catalytic N-terminal domain	8026008	4001185	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Galactose mutarotase-like	8041536	3000035	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Hyaluronate lyase-like C-terminal domain	8041256	3001435	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Chondroitin AC/alginate lyase	8038387	3001005	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	Lyase_8_C_1	e1cb8A1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Hyaluronate lyase-like, C-terminal domain (From Topology)	T: Hyaluronate lyase-like, C-terminal domain	F: Lyase_8_C_1	ECOD (1.6)
A	Lyase_8	e1cb8A2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Lyase_8	ECOD (1.6)
A	Lyase_8_N	e1cb8A3	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Lyase_8_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.50.10.100	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase	Chondroitin AC/alginate lyase	CATH (4.3.0)
A	2.70.98.10	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
A	2.60.220.10	Mainly Beta	Sandwich	Chondroitinase Ac	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08124	Polysaccharide lyase family 8, N terminal alpha-helical domain (Lyase_8_N)	Polysaccharide lyase family 8, N terminal alpha-helical domain	-	Repeat
A	PF02278	Polysaccharide lyase family 8, super-sandwich domain (Lyase_8)	Polysaccharide lyase family 8, super-sandwich domain	-	Family
A	PF02884	Polysaccharide lyase family 8, C-terminal beta-sandwich domain (Lyase_8_C)	Polysaccharide lyase family 8, C-terminal beta-sandwich domain	This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN (CHONDROITINASE AC)	binding carbohydrate binding lyase activity carbon-oxygen lyase activity, acting on polysaccharides catalytic activity carbon-oxygen lyase activity chondroitin AC lyase activity cation binding ion binding metal ion binding small molecule binding	carbohydrate metabolic process organic substance metabolic process primary metabolic process metabolic process	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011071	Polysaccharide lyase family 8-like, C-terminal	Homologous Superfamily
A	IPR012970	Polysaccharide lyase 8, N-terminal alpha-helical	Domain
A	IPR004103	Polysaccharide lyase family 8, C-terminal	Domain
A	IPR038970	Polysaccharide lyase 8	Family
A	IPR003159	Polysaccharide lyase family 8, central domain	Domain
A	IPR008929	Chondroitin AC/alginate lyase	Homologous Superfamily
A	IPR014718	Glycoside hydrolase-type carbohydrate-binding	Homologous Superfamily
A	IPR011013	Galactose mutarotase-like domain superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	chondroitin AC lyase M-CSA #441	Glycosaminoglycans (GAGs) are highly negatively charged polysaccharides, formed from disaccharide repeating units. For a number of bacterial species, including Flavobacterium heparinum synthesise GAG lyases, these enzymes are used to degrade and utilise glycosaminoglycans as a source of carbon in the bacterium's natural environment. This enzyme from Flavobacterium heparinum is highly activated to chondroitin 4-sulfate and chondroitin 6-sulfate. These GAGs are major components of the extracellular matrix. The enzyme consists of two domains, a C-terminal domain containing a 4-beta-sheet sandwich, and an N-terminal domain containing the active site which is made up of alpha-helices. Although calcium is known to be activating, it is not yet clear if it is actively involved in the catalytic mechanism or in substrate binding/recognition.	Defined by 5 residues: ASN:A-153 [auth A-175]HIS:A-203 [auth A-225]TYR:A-212 [auth A-234]ARG:A-266 [auth A-288]GLU:A-349 [auth A-371] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.2.2.5 (PDB Primary Data) Search M-CSA Motif + EC 4.2.2.5

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.