A0A5D8YFB0 · A0A5D8YFB0_9SPHI
- ProteinGlutamine-dependent NAD(+) synthetase
- GenenadE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids546 (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
- deamido-NAD+ + L-glutamine + ATP + H2O = L-glutamate + AMP + diphosphate + NAD+ + H+
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 | 41 | Proton acceptor | |||
Active site | 41 | Proton acceptor; for glutaminase activity | |||
Active site | 112 | For glutaminase activity | |||
Binding site | 118 | L-glutamine (UniProtKB | ChEBI) | |||
Active site | 148 | Nucleophile; for glutaminase activity | |||
Binding site | 182 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 295-302 | ATP (UniProtKB | ChEBI) | |||
Binding site | 378 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | |||
Binding site | 402 | ATP (UniProtKB | ChEBI) | |||
Binding site | 407 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | |||
Binding site | 517 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | |||
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 > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter
Accessions
- Primary accessionA0A5D8YFB0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-257 | CN hydrolase | |||
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
- Length546
- Mass (Da)60,564
- Last updated2019-11-13 v1
- Checksum4E33BB1CBE5D8788
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VTRT01000014 EMBL· GenBank· DDBJ | TZF80917.1 EMBL· GenBank· DDBJ | Genomic DNA |