| Analysis | rpsblast_cdd | Start | 63 |
| End | 193 | Strand | + |
| Length | 131 | Note | Gaps:13 |
| Hit Coverage | 90.65 | Hit Length | 139 |
| Hit Pident | 26.98 | E Val | 2e-13 |
| 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 | 20.63 |
| Name | Qrob_P0264740.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0264740.2 | Quercus robur | 100.0 | egn | (M=1) PTHR11748//PTHR11748:SF16 - D-LACTATE DEHYDROGENASE // SUBFAMILY NOT NAMED | EC:1.1.3.8, EC:1.1.3.37 | validated |
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