2BKX

Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the NagB superfamily

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8074892	3000693	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8074892	3000693	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	Glucosamine_iso	e2bkxA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: Glucosamine_iso	ECOD (1.6)
B	Glucosamine_iso	e2bkxB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: Glucosamine_iso	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01182	Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase (Glucosamine_iso)	Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GLUCOSAMINE-6-PHOSPHATE DEAMINASE	glucosamine-6-phosphate deaminase activity hydrolase activity deaminase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds identical protein binding protein binding binding	carbohydrate derivative catabolic process catabolic process amino sugar catabolic process glucosamine catabolic process amino sugar metabolic process carbohydrate derivative metabolic process metabolic process glucosamine metabolic process glucosamine-containing compound metabolic process glucosamine-containing compound catabolic process carbohydrate metabolic process primary metabolic process N-acetylglucosamine catabolic process N-acetylglucosamine metabolic process carbohydrate derivative catabolic process catabolic process amino sugar catabolic process glucosamine catabolic process amino sugar metabolic process carbohydrate derivative metabolic process metabolic process glucosamine metabolic process glucosamine-containing compound metabolic process glucosamine-containing compound catabolic process carbohydrate metabolic process primary metabolic process N-acetylglucosamine catabolic process N-acetylglucosamine metabolic process N-acetylneuraminate catabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process organic acid catabolic process organic acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process cellular process amide metabolic process small molecule catabolic process N-acetylneuraminate metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR006148	Glucosamine/galactosamine-6-phosphate isomerase	Domain
A, B	IPR004547	Glucosamine-6-phosphate isomerase	Family
A, B	IPR018321	Glucosamine-6-phosphate isomerase, conserved site	Conserved Site
A, B	IPR037171	NagB/RpiA transferase-like	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.