3TBF

C-terminal domain of glucosamine-fructose-6-phosphate aminotransferase from Francisella tularensis.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3tbfa_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
B	d3tbfb_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
C	d3tbfc_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
D	d3tbfd_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
E	d3tbfe_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
F	d3tbff_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
G	d3tbfg_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)
H	d3tbfh_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	double-SIS domain	automated matches	(Francisella tularensis subsp. tularensis ) [TaxId: 119856 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	SIS_3	e3tbfA2	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	SIS_3	e3tbfB2	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	SIS_3	e3tbfC2	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)
D	SIS_3	e3tbfD2	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)
E	SIS_3	e3tbfE2	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)
F	SIS_3	e3tbfF2	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)
G	SIS_3	e3tbfG2	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)
H	SIS_3	e3tbfH2	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	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	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	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
D	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
E	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
F	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
G	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
H	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, D, E A, B, C, D, E, F, G, H	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]	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	carbohydrate derivative biosynthetic process glycoprotein biosynthetic process carbohydrate derivative metabolic 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 carbohydrate derivative biosynthetic process glycoprotein biosynthetic process carbohydrate derivative metabolic 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 protein metabolic process macromolecule metabolic process protein modification process organophosphate metabolic process phosphate-containing compound metabolic process fructose 6-phosphate metabolic process phosphorus metabolic process carbohydrate metabolic process nucleoside phosphate metabolic process nucleotide-sugar metabolic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process amino sugar metabolic process small molecule metabolic process UDP-N-acetylglucosamine metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

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

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.