| Analysis | rpsblast_cdd | Start | 28 |
| End | 78 | Strand | + |
| Length | 51 | Note | none |
| Hit Coverage | 20.08 | Hit Length | 254 |
| Hit Pident | 37.25 | E Val | 1e-07 |
| Hit Description | cd07576 R-amidase_like Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases). Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup 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) class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer. | Hit Pcons | 11.76 |
| Name | Qrob_P0619140.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0619140.2 | Quercus robur | 100.0 | egn | (M=3) 3.5.5.1//3.5.5.4 - Nitrilase. // Cyanoalanine nitrilase. | EC:3.5.5.4, EC:3.5.5.1 | validated |
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