| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_10430302g0010 |
| Family | AA7 |
| Protein Properties | Length: 221 Molecular Weight: 24168.7 Isoelectric Point: 8.1211 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| AA7 | 62 | 221 | 0 |
| QNLRYTEHSVRKPYVLIVPQSRQQVQKTVVCCIKHGWEIRVRSGGHSYEGLSSTSDIPFVIIDLMNLDAINIDLATKTAWVEAGATVGQLYDAIANTTAI YGFPAGVCSTMGTGGHFSGGGLSLLSRKHGIAADNIIDALFVDARGNLLNRQKMGKDVFW | |||
| Full Sequence |
|---|
| Protein Sequence Length: 221 Download |
| MAFFGYLKWL SICSFLFCQL VVAAVSVQDG LISCLTRNAI TNFTTSFSSS SEYYSLLNFS 60 VQNLRYTEHS VRKPYVLIVP QSRQQVQKTV VCCIKHGWEI RVRSGGHSYE GLSSTSDIPF 120 VIIDLMNLDA INIDLATKTA WVEAGATVGQ LYDAIANTTA IYGFPAGVCS TMGTGGHFSG 180 GGLSLLSRKH GIAADNIIDA LFVDARGNLL NRQKMGKDVF W |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02465 | PLN02465 | 0.007 | 80 | 156 | 78 | + L-galactono-1,4-lactone dehydrogenase | ||
| COG0277 | GlcD | 1.0e-13 | 72 | 211 | 143 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 6.0e-21 | 74 | 211 | 139 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAU20769.1 | 0 | 10 | 221 | 2 | 215 | berberine bridge enzyme [Thalictrum flavum subsp. glaucum] |
| GenBank | ACO90218.1 | 0 | 16 | 221 | 13 | 218 | berberine bridge enzyme [Eschscholzia californica] |
| GenBank | ACO90226.1 | 0 | 15 | 221 | 5 | 213 | putative berberine bridge enzyme [Papaver bracteatum] |
| GenBank | ACO90228.1 | 0 | 15 | 221 | 19 | 230 | berberine bridge enzyme-like protein [Papaver bracteatum] |
| Swiss-Prot | P93479 | 0 | 10 | 221 | 6 | 222 | RETO_PAPSO RecName: Full=Reticuline oxidase; AltName: Full=Berberine bridge-forming enzyme; Short=BBE; AltName: Full=Tetrahydroprotoberberine synthase; Flags: Precursor |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3d2j_A | 0 | 16 | 221 | 13 | 218 | A Chain A, Bacillus Subtilis Pectate Lyase R279k Mutant |
| PDB | 3d2h_A | 0 | 16 | 221 | 13 | 218 | A Chain A, Bacillus Subtilis Pectate Lyase R279k Mutant |
| PDB | 3d2d_A | 0 | 16 | 221 | 13 | 218 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
| PDB | 3fw9_A | 0 | 31 | 221 | 2 | 193 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 4ec3_A | 0 | 29 | 221 | 6 | 199 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
