A0A0Q4E1L2 · A0A0Q4E1L2_9SPHN
- ProteinGlutamine-dependent NAD(+) synthetase
- GenenadE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids681 (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 | 54 | Proton acceptor; for glutaminase activity | ||||
Sequence: E | ||||||
Active site | 123 | For glutaminase activity | ||||
Sequence: K | ||||||
Binding site | 129 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 179 | Nucleophile; for glutaminase activity | ||||
Sequence: C | ||||||
Binding site | 206 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 212 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 369-376 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GVSGGLDS | ||||||
Binding site | 459 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: N | ||||||
Binding site | 483 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 488 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: E | ||||||
Binding site | 493-496 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: WSTY | ||||||
Binding site | 639 | 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 | |
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 > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas
Accessions
- Primary accessionA0A0Q4E1L2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-279 | CN hydrolase | ||||
Sequence: IRVAAATPRASVGDTGANAEATIALAREADAKGVDLVVFPELNLTSYAIDDLHLQTAQQRATLAAIGTVVEASAILRPVLLVGAALVRNGRLYNCALAIARGHVLGVVPKTFLPNYREFYEKRWFASGMGMTGLTIDLDGEAIPFGTDLIFAARDLPGFVFHAEICEDYWAPTPPSTAGALAGALICCNLSASNIVIGKARDRAMLAAAQSARAVCAYVYSAAGPGESTTEVAWDGQGLVHELGEQIAESARFSTEPELVVADVDC | ||||||
Region | 644-663 | Disordered | ||||
Sequence: PNGPKVSAGGALSPRGDWRA |
Sequence similarities
In the C-terminal section; belongs to the NAD synthetase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length681
- Mass (Da)73,672
- Last updated2016-01-20 v1
- Checksum72B45F361BA0999D