2POC

The crystal structure of isomerase domain of glucosamine-6-phosphate synthase from Candida albicans

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	d2poca_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Candida albicans SC5314 ) [TaxId: 237561 ],	SCOPe (2.08)
C	d2pocc_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Candida albicans SC5314 ) [TaxId: 237561 ],	SCOPe (2.08)
B	d2pocb_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Candida albicans SC5314 ) [TaxId: 237561 ],	SCOPe (2.08)
D	d2pocd_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	automated matches	automated matches	(Candida albicans SC5314 ) [TaxId: 237561 ],	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	e2pocA2	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	e2pocC1	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	e2pocB1	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	e2pocD2	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)
C	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)
D	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	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	isomerase domain of glutamine-fructose-6-phosphate transaminase (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 amino sugar biosynthetic process glucosamine biosynthetic process glucosamine metabolic process glucosamine-containing compound biosynthetic process amino sugar metabolic process glucosamine-containing compound metabolic process nucleoside phosphate metabolic process nucleotide-sugar metabolic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process small molecule metabolic process UDP-N-acetylglucosamine metabolic process nucleobase-containing compound biosynthetic process UDP-N-acetylglucosamine biosynthetic process organophosphate biosynthetic process nucleoside phosphate 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 growth filamentous growth hyphal growth chitin biosynthetic process chitin metabolic process aminoglycan metabolic process aminoglycan biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

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