A0A0E3LIX5 · A0A0E3LIX5_9EURY
- ProteinNH(3)-dependent NAD(+) synthetase
- GenenadE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids265 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic activity
- deamido-NAD+ + NH4+ + ATP = AMP + diphosphate + NAD+ + H+
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; NAD+ from deamido-NAD+ (ammonia route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 39-46 | ATP (UniProtKB | ChEBI) | |||
Binding site | 45 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 125 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | |||
Binding site | 145 | ATP (UniProtKB | ChEBI) | |||
Binding site | 150 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 158 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | |||
Binding site | 165 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits | |||
Binding site | 174 | ATP (UniProtKB | ChEBI) | |||
Binding site | 196 | ATP (UniProtKB | ChEBI) | |||
Binding site | 255-256 | deamido-NAD+ (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | glutaminase activity | |
Molecular Function | metal ion binding | |
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 nameNH(3)-dependent NAD(+) synthetase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinaceae > Methanosarcina
Accessions
- Primary accessionA0A0E3LIX5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length265
- Mass (Da)28,870
- Last updated2015-06-24 v1
- Checksum46CAD3F32EC8E0E4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP009524 EMBL· GenBank· DDBJ | AKB46781.1 EMBL· GenBank· DDBJ | Genomic DNA |