5KHA

Structure of glutamine-dependent NAD+ synthetase from Acinetobacter baumannii in complex with adenosine diphosphate (ADP)

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	CN_hydrolase	e5khaA1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: CN_hydrolase	ECOD (1.6)
A	NAD_synthase	e5khaA2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: NAD_synthase	ECOD (1.6)
B	CN_hydrolase	e5khaB1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Carbon-nitrogen hydrolase (From Topology)	T: Carbon-nitrogen hydrolase	F: CN_hydrolase	ECOD (1.6)
B	NAD_synthase	e5khaB2	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: NAD_synthase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
B	3.60.110.10	Alpha Beta	4-Layer Sandwich	Nitrilase/N-carbamoyl-D-aminoacid amidohydrolase	Carbon-nitrogen hydrolase	CATH (4.3.0)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02540	NAD synthase (NAD_synthase)	NAD synthase	NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.	Domain
A, B	PF00795	Carbon-nitrogen hydrolase (CN_hydrolase)	Carbon-nitrogen hydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Glutamine-dependent NAD+ synthetase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding NAD+ synthase (glutamine-hydrolyzing) activity carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides glutaminase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds transferase activity acid-ammonia (or amide) ligase activity NAD+ synthase activity	glutamine metabolic process organonitrogen compound metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary 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 organic substance metabolic process metabolic process glutamine metabolic process organonitrogen compound metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary 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 organic substance metabolic process metabolic process small molecule metabolic process cellular process nucleotide biosynthetic process organonitrogen compound biosynthetic process NAD metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process organic substance biosynthetic process pyridine-containing compound metabolic process phosphorus metabolic process pyridine nucleotide metabolic process NAD biosynthetic process pyridine nucleotide biosynthetic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process pyridine-containing compound biosynthetic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nicotinamide nucleotide biosynthetic process organic cyclic compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process purine nucleotide biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR022310	NAD/GMP synthase	Domain
A, B	IPR014445	Glutamine-dependent NAD(+) synthetase	Family
A, B	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
A, B	IPR003010	Carbon-nitrogen hydrolase	Domain
A, B	IPR036526	Carbon-nitrogen hydrolase superfamily	Homologous Superfamily
A, B	IPR003694	NAD(+) synthetase	Family

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.