1JXA

GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE

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	d1jxaa1	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	'Isomerase domain' of glucosamine 6-phosphate synthase (GLMS)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1jxaa2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	Glucosamine 6-phosphate synthase, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1jxab1	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	'Isomerase domain' of glucosamine 6-phosphate synthase (GLMS)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1jxab2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	Glucosamine 6-phosphate synthase, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1jxac1	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	'Isomerase domain' of glucosamine 6-phosphate synthase (GLMS)	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1jxac2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Class II glutamine amidotransferases	Glucosamine 6-phosphate synthase, N-terminal domain	(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)
A	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8052796	3001397	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Class II glutamine amidotransferases	8041848	3000131	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8032993	3001397	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8052796	3001397	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8032993	3001397	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Class II glutamine amidotransferases	8041848	3000131	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class II glutamine amidotransferases	8041848	3000131	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8032993	3001397	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8052796	3001397	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	GATase_2_1st	e1jxaA5	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: GATase_2_1st	ECOD (1.6)
A	SIS_3	e1jxaA3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS_3	ECOD (1.6)
B	GATase_2_1st	e1jxaB5	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: GATase_2_1st	ECOD (1.6)
B	SIS_3	e1jxaB3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS_3	ECOD (1.6)
C	GATase_2_1st	e1jxaC5	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Class II glutamine amidotransferases	F: GATase_2_1st	ECOD (1.6)
C	SIS_3	e1jxaC3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
A	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
B	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
B	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
C	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
C	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01380	SIS domain (SIS)	SIS domain	SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domain ...	SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.	Domain
A, B, C	PF13522	Glutamine amidotransferase domain (GATase_6)	Glutamine amidotransferase domain	This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	glucosamine 6-phosphate synthase	binding carbohydrate derivative binding transferase activity, transferring nitrogenous groups glutamine-fructose-6-phosphate transaminase (isomerizing) activity L-glutamine aminotransferase activity transaminase activity transferase activity catalytic activity	cellular biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process protein modification process carbohydrate derivative biosynthetic process organonitrogen compound metabolic process cellular metabolic process glycoprotein biosynthetic process primary metabolic process glycoprotein metabolic process protein N-linked glycosylation cellular biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process protein modification process carbohydrate derivative biosynthetic process organonitrogen compound metabolic process cellular metabolic process glycoprotein biosynthetic process primary metabolic process glycoprotein metabolic process protein N-linked glycosylation protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation metabolic process cellular process macromolecule metabolic process organophosphate metabolic process phosphate-containing compound metabolic process fructose 6-phosphate metabolic process phosphorus metabolic process carbohydrate metabolic process nucleotide-sugar metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process nucleobase-containing small molecule metabolic process amino sugar metabolic process small molecule metabolic process UDP-N-acetylglucosamine metabolic process amino sugar biosynthetic process nucleobase-containing compound biosynthetic process UDP-N-acetylglucosamine biosynthetic process organic cyclic compound biosynthetic process nucleotide-sugar biosynthetic process glutamine metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process glutamine family amino acid metabolic process proteinogenic amino acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR046348	SIS domain superfamily	Homologous Superfamily
A, B, C	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, B, C	IPR035466	GlmS/AgaS, SIS domain 1	Domain
A, B, C	IPR005855	Glucosamine-fructose-6-phosphate aminotransferase, isomerising	Family
A, B, C	IPR035490	GlmS/FrlB, SIS domain 2	Domain
A, B, C	IPR017932	Glutamine amidotransferase type 2 domain	Domain
A, B, C	IPR047084	Glucosamine-fructose-6-phosphate aminotransferase, isomerising, N-terminal domain	Domain
A, B, C	IPR001347	SIS domain	Domain

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

Chains	Enzyme Name	Description	Catalytic Residues
A	glutamine-fructose-6-phosphate transaminase (isomerizing) M-CSA #82	Glucosamine-fructose-6-phosphate aminotransferase (isomerizing) also known as Glucosamine-6-phosphate synthase (GlmS), catalyses the first reaction in hexamine biosynthesis. It belongs to an F-type group of glutamine-dependent amidotransferase family of enzymes, which utilise the glutamine amide nitrogen in the biosynthesis of phosphoribosylamine, glutamate or asparagine. The hexosamine biosynthetic pathway starts from D fructose-6-phosphate (Fru6P)2 which is produced from glucose via the glycolysis pathway. The Fru6P is converted into D -glucosamine-6-phosphate (GlcN6P) by the rate-limiting enzyme glucosamine-6-phosphate synthase (GlcN6P synthase). This is the sole biosynthetic route to GlcN6P known to date. The reaction is practically irreversible and the reaction takes place over two structural domains, an N-terminal glutaminase domain, which hydrolyses glutamine to glutamate and ammonia (residues 1-240), and a C-terminal isomerase domain (residues 241-608), which catalyses the ketose-aldose isomerisation and utilises the nitrogen for synthesis of GlcN-6P. The isomerase domain is responsible for two activities of GlmS, the conversion of Fru-6P into GlcN-6P in the presence of glutamine (the synthase activity), and the isomerisation of Fru-6P into Glc-6P (the phosphoglucose isomerase - like activity) in the absence of glutamine. The product of the reaction with fructose 6-phosphate, glucosamine 6-phosphate, undergoes transformation leading towards formation of uridine diphospho-N-acetylglucosamine - which is a precursor to all amino sugar-containing macromolecules. Much interest has been shown in this enzyme that is believed to have important implications in antibacterial/antifungal therapy and diabetes treatment.	Defined by 10 residues: CYS:A-1ARG:A-26TRP:A-74ASN:A-98GLY:A-99GLU:A-481LYS:A-485GLU:A-488HIS:A_2-504LYS:A-603 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.6.1.16 (PDB Primary Data) Search M-CSA Motif + EC 2.6.1.16

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.