5HJ5

Crystal structure of tertiary complex of glucosamine-6-phosphate deaminase from Vibrio cholerae with BETA-D-GLUCOSE-6-PHOSPHATE and FRUCTOSE-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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5hj5a_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	NagB-like	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
B	d5hj5b1	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	NagB-like	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
B	d5hj5b2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
C	d5hj5c_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	NagB-like	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)
D	d5hj5d_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	NagB-like	automated matches	(Vibrio cholerae O1 biovar El Tor str. N16961 ) [TaxId: 243277 ],	SCOPe (2.08)

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	8074888	3000693	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8074888	3000693	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8074888	3000693	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8074888	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	e5hj5A1	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	e5hj5B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: Glucosamine_iso	ECOD (1.6)
C	Glucosamine_iso	e5hj5C1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: Glucosamine_iso	ECOD (1.6)
D	Glucosamine_iso	e5hj5D1	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)
C	3.40.50.1360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	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, C, D	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, C, D	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 organonitrogen compound catabolic process N-acetylneuraminate catabolic process organonitrogen compound metabolic 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, C, D	IPR006148	Glucosamine/galactosamine-6-phosphate isomerase	Domain
A, B, C, D	IPR004547	Glucosamine-6-phosphate isomerase	Family
A, B, C, D	IPR018321	Glucosamine-6-phosphate isomerase, conserved site	Conserved Site
A, B, C, D	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 R01GM133198.