| Analysis | rpsblast_cdd | Start | 69 |
| End | 252 | Strand | + |
| Length | 184 | Note | Gaps:26 |
| Hit Coverage | 95.56 | Hit Length | 180 |
| Hit Pident | 33.72 | E Val | 3e-29 |
| Hit Description | cd02064 FAD_synthetase_N FAD synthetase N-terminal domain of the bifunctional enzyme. FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However the bifunctional enzyme is not found in mammals which use separate enzymes for FMN and FAD formation. | Hit Pcons | 20.35 |
| Name | Qrob_P0029080.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0029080.2 | Quercus robur | 100.0 | egn | (M=2) 2.7.7.2 - FAD synthetase. | EC:2.7.7.2 | validated |
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