Annotations: 2D2X

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dehydroquinate synthase-like	8100644	3001905	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Dehydroquinate synthase-like	8100644	3001905	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	DHQ_synthase_C	e2d2xA2	A: alpha bundles	X: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	H: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	T: alpha-helical domain in dehydroquinate synthase-like enzymes	F: DHQ_synthase_C	ECOD (1.6)
A	DHQ_synthase_N	e2d2xA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Rossmann-like domain in dehydroquinate synthase-like enzymes	F: DHQ_synthase_N	ECOD (1.6)
B	DHQ_synthase_C	e2d2xB1	A: alpha bundles	X: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	H: alpha-helical domain in dehydroquinate synthase-like enzymes (From Topology)	T: alpha-helical domain in dehydroquinate synthase-like enzymes	F: DHQ_synthase_C	ECOD (1.6)
B	DHQ_synthase_N	e2d2xB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Rossmann-like domain in dehydroquinate synthase-like enzymes	F: DHQ_synthase_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	1.20.1090.10	Mainly Alpha	Up-down Bundle	Dehydroquinate synthase-like, alpha domain	Dehydroquinate synthase-like - alpha domain	CATH (4.3.0)
B	3.40.50.1970	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	1.20.1090.10	Mainly Alpha	Up-down Bundle	Dehydroquinate synthase-like, alpha domain	Dehydroquinate synthase-like - alpha domain	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	2-deoxy-scyllo-inosose synthase	carbon-oxygen lyase activity, acting on phosphates lyase activity catalytic activity carbon-oxygen lyase activity cation binding ion binding binding metal ion binding small molecule binding	organonitrogen compound metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic cyclic compound metabolic process organonitrogen compound metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic cyclic compound metabolic process organic substance metabolic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process small molecule metabolic process metabolic process cellular process antibiotic metabolic process antibiotic biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR030960	3-dehydroquinate synthase domain	Domain
A, B	IPR030963	3-dehydroquinate synthase family	Family

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.