A0A023X657 · A0A023X657_RUBRA
- ProteinGlutamine-dependent NAD(+) synthetase
- GenenadE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids600 (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 | 60 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 60 | Proton acceptor; for glutaminase activity | ||||
Sequence: E | ||||||
Active site | 127 | For glutaminase activity | ||||
Sequence: K | ||||||
Binding site | 133 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 163 | Nucleophile; for glutaminase activity | ||||
Sequence: C | ||||||
Binding site | 190 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 196 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 338-345 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLSGGVDS | ||||||
Binding site | 421 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: N | ||||||
Binding site | 445 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 450 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: E | ||||||
Binding site | 562 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Rubrobacteria > Rubrobacterales > Rubrobacteraceae > Rubrobacter
Accessions
- Primary accessionA0A023X657
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-260 | CN hydrolase | ||||
Sequence: MRVALAQVNTTVGDIWGNVEKLSEALGRAVESGADLVAFPELALTGYPPEDLLLRPGFIGDNLKALEEFRACVPEDVVAAVGFVDLGLDLFNACAVISGGEVLDRYHKRYLPNYGVFDENRYFREGTGSSLLDLDGTLVGVNVCEDIWYPGGPGREQALGGASVLVNVSASPYHRLKGATRERMLSVRASDYGCYVVMCNLVGGQDELVFDGHSVVFDPEGELVARAKQFEEDLLLVDIFP |
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
- Length600
- Mass (Da)65,935
- Last updated2014-07-09 v1
- Checksum7291F9822B054BF2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP007514 EMBL· GenBank· DDBJ | AHY47691.1 EMBL· GenBank· DDBJ | Genomic DNA |