1DEA

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

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)
B	d1deab_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	NagB-like	Glucosamine 6-phosphate deaminase/isomerase NagB	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1deaa_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	NagB-like	Glucosamine 6-phosphate deaminase/isomerase NagB	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8035696	3000693	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8035696	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)
B	Glucosamine_iso	e1deaB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: Glucosamine_iso	ECOD (1.6)
A	Glucosamine_iso	e1deaA1	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)
B	3.40.50.1360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	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 carbohydrate derivative metabolic process glucosamine metabolic process glucosamine-containing compound catabolic process amino sugar catabolic process glucosamine catabolic process amino sugar metabolic process metabolic process cellular process glucosamine-containing compound metabolic process carbohydrate metabolic process primary metabolic process N-acetylneuraminate catabolic process carbohydrate derivative catabolic process catabolic process carbohydrate derivative metabolic process glucosamine metabolic process glucosamine-containing compound catabolic process amino sugar catabolic process glucosamine catabolic process amino sugar metabolic process metabolic process cellular process glucosamine-containing compound metabolic process carbohydrate metabolic process primary metabolic process N-acetylneuraminate catabolic process oxoacid 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 amide metabolic process small molecule catabolic process N-acetylneuraminate metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process amino sugar biosynthetic process nucleotide-sugar metabolic process nucleobase-containing compound biosynthetic process UDP-N-acetylglucosamine biosynthetic process nucleobase-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleobase-containing small molecule metabolic process nucleoside phosphate biosynthetic process phosphate-containing compound metabolic process nucleotide-sugar biosynthetic process phosphorus metabolic process UDP-N-acetylglucosamine metabolic process N-acetylglucosamine metabolic process N-acetylglucosamine catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

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

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

Chains	Enzyme Name	Description	Catalytic Residues
A	glucosamine-6-phosphate deaminase M-CSA #60	The allosteric hexameric enzyme from Escherichia coli catalyses the regulatory step of N-acetyl glucosamine catabolism, which consists of the isomerisation and deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonia.The enzyme is a hexamer of identical subunits arranged as a dimer of trimers and the allosteric sites appear located in the clefts between the subunits forming the trimers. Glucosamine-6-phosphate isomerase is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The allosteric transition from T to R is generated upon binding of GlcNAc6P at the allosteric site or binding of active-site ligands (GlcN6P, Fru6P, GlcN-ol-6P). An important local conformational change relating allosteric control to catalysis is centred on residue Glu148. Glu148 participates in a proton-relay system that serves to polarise His143. This histidine is essential for the catalytic ring opening of the GlcN6P substrate. The His143 is primarily activated by its interaction with Glu148. The second residue in the His-Glu-Asx triangle appears to be either an Asp or Asn. Interestingly enough, in the work on Escherichia coli, Asn in this position severely disrupts the enzyme's activity.	Defined by 4 residues: ASP:A-72ASP:A-141HIS:A-143GLU:A-148 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.99.6 (UniProt) Search M-CSA Motif + EC 3.5.99.6

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.