| Analysis | rpsblast_cdd | Start | 5 |
| End | 68 | Strand | + |
| Length | 64 | Note | none |
| Hit Coverage | 24.52 | Hit Length | 261 |
| Hit Pident | 35.94 | E Val | 4e-18 |
| Hit Description | cd07570 GAT_Gln-NAD-synth Glutamine aminotransferase (GAT glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases). Glutamine-dependent NAD synthetases are bifunctional enzymes which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13) this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer. | Hit Pcons | 15.62 |
| Name | Qrob_P0374880.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0374880.2 | Quercus robur | 46.9 | egn | (M=2) 6.3.5.1 - NAD(+) synthase (glutamine-hydrolyzing). | EC:6.3.5.1 | validated |
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