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	PF01182	e5hj5A1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: PF01182	ECOD (1.6)
B	PF01182	e5hj5B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: PF01182	ECOD (1.6)
C	PF01182	e5hj5C1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: PF01182	ECOD (1.6)
D	PF01182	e5hj5D1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: PF01182	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 carbohydrate derivative metabolic process glucosamine metabolic process glucosamine-containing compound catabolic process organic substance metabolic process amino sugar catabolic process glucosamine catabolic process amino sugar metabolic process metabolic process organic substance catabolic process glucosamine-containing compound metabolic process carbohydrate metabolic process primary metabolic process carbohydrate derivative catabolic process catabolic process carbohydrate derivative metabolic process glucosamine metabolic process glucosamine-containing compound catabolic process organic substance metabolic process amino sugar catabolic process glucosamine catabolic process amino sugar metabolic process metabolic process organic substance catabolic process glucosamine-containing compound metabolic process carbohydrate metabolic process primary metabolic process N-acetylglucosamine metabolic process N-acetylglucosamine catabolic process oxoacid metabolic process organic acid catabolic process organic acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amide metabolic process N-acetylneuraminate metabolic process organonitrogen compound catabolic process N-acetylneuraminate catabolic process organonitrogen compound metabolic process cellular metabolic process carboxylic acid metabolic process cellular process small molecule catabolic 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.