| Analysis | rpsblast_cdd | Start | 74 |
| End | 148 | Strand | + |
| Length | 75 | Note | Gaps:4 |
| Hit Coverage | 56.83 | Hit Length | 139 |
| Hit Pident | 35.44 | E Val | 4e-09 |
| Hit Description | pfam01565 FAD_binding_4 FAD binding domain. This family consists of various enzymes that use FAD as a co-factor most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure the alignment includes the FAD binding site called the PP-loop between residues 99-110. The FAD molecule is covalently bound in the known structure however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor mitomycin radical oxidase this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | Hit Pcons | 15.19 |
| Name | Qrob_P0428470.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0428470.2 | Quercus robur | 56.0 | egn | (M=27) 1.3.3.8 - Tetrahydroberberine oxidase. | EC:1.3.3.8 | validated |
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