A0A3A9ZCN3 · A0A3A9ZCN3_9ACTN
- ProteinGlutamine-dependent NAD(+) synthetase
- GenenadE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids615 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic activity
- ATP + deamido-NAD+ + H2O + L-glutamine = AMP + diphosphate + H+ + L-glutamate + NAD+
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; NAD+ from deamido-NAD+ (L-Gln route): step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 72 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 72 | Proton acceptor; for glutaminase activity | ||||
Sequence: E | ||||||
Active site | 154 | For glutaminase activity | ||||
Sequence: K | ||||||
Binding site | 160 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 190 | Nucleophile; for glutaminase activity | ||||
Sequence: C | ||||||
Binding site | 217 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 223 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 359-366 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLSGGVDS | ||||||
Binding site | 436 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: N | ||||||
Binding site | 465 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: E | ||||||
Binding site | 581 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | glutaminase activity | |
Molecular Function | NAD+ synthase (glutamine-hydrolyzing) activity | |
Molecular Function | NAD+ synthase activity | |
Molecular Function | nitrilase activity | |
Biological Process | NAD biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamine-dependent NAD(+) synthetase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A3A9ZCN3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-287 | CN hydrolase | ||||
Sequence: LRLALNQIDSTVGDLPGNADAVLRWTRHGVERGAHLVVFPEMMLTGYPVEDLALRSSFVSAAREALRGLAARLAAEGLGETPVLLGYLDRAEAVPERPWQPVGTPQNAAAVLHRGRVVLSFAKHHLPNYGVFDEFRYFVPGETLPVVRVHGVDVALAICEDLWQDGGRVPAARAAGAGLLVAINASPYEVAKEDVRLDLVRKRAQEAGCTLAYLAMTGGQDELVYDGDSLVVDRNGEVLLRGPQFEEECLLVDLEL | ||||||
Region | 504-531 | Disordered | ||||
Sequence: AERGETPPIPENTLVKPPSAELRPGQVD |
Sequence similarities
Belongs to the NAD synthetase family.
In the C-terminal section; belongs to the NAD synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length615
- Mass (Da)66,634
- Last updated2018-12-05 v1
- ChecksumE8C0A6BACFFD64B7
Keywords
- Technical term