| Basic Information | |
|---|---|
| Species | Prunus persica |
| Cazyme ID | ppa023762m |
| Family | AA7 |
| Protein Properties | Length: 423 Molecular Weight: 46675 Isoelectric Point: 5.2999 |
| Chromosome | Chromosome/Scaffold: 4 Start: 20164531 End: 20165799 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 2 | 406 | 0 |
| NLNRVSVDLETETAWVEGGATLGETYHAIAKASLVHGFSAGSCPTVGVGGHIAGGGFGLMSRKYGLAADNVVDALLVDAEGRLLDREGMGDDVFWAIRGG GGGVWGVVYSWKIQLLKVPQIVTAFVVSRPGEKRHVAKLVDKWQNVSPYLEDDFYISCFVGAGLPEAKNATSPSGISATFKGFYLGPRSTAMSILNQAFP DLGITQDDCTEMSWIESVVFFSGLSKGSLVSDLRNRYLQEKGYFKAKSDYVRTPISQAGIEAAIEILEEEPKGYVILDPYGGIMHHVSSESIAFPHRKGN LFTIQYLVEWKEEDNYKKDDYIDWIRRLYNSMTQFVSWDPRAAYINYVDLDLGTMRFVDPSVTTKDAVEIARDWGEKYFLNNYNRLVKAKTLIDPSNVFR NQQGI | |||
| Full Sequence |
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| Protein Sequence Length: 423 Download |
| MNLNRVSVDL ETETAWVEGG ATLGETYHAI AKASLVHGFS AGSCPTVGVG GHIAGGGFGL 60 MSRKYGLAAD NVVDALLVDA EGRLLDREGM GDDVFWAIRG GGGGVWGVVY SWKIQLLKVP 120 QIVTAFVVSR PGEKRHVAKL VDKWQNVSPY LEDDFYISCF VGAGLPEAKN ATSPSGISAT 180 FKGFYLGPRS TAMSILNQAF PDLGITQDDC TEMSWIESVV FFSGLSKGSL VSDLRNRYLQ 240 EKGYFKAKSD YVRTPISQAG IEAAIEILEE EPKGYVILDP YGGIMHHVSS ESIAFPHRKG 300 NLFTIQYLVE WKEEDNYKKD DYIDWIRRLY NSMTQFVSWD PRAAYINYVD LDLGTMRFVD 360 PSVTTKDAVE IARDWGEKYF LNNYNRLVKA KTLIDPSNVF RNQQGIPPMS LAGLSSVLHA 420 EI* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| COG0277 | GlcD | 4.0e-6 | 3 | 131 | 136 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
| pfam01565 | FAD_binding_4 | 2.0e-11 | 3 | 86 | 85 | + 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. |
| pfam08031 | BBE | 3.0e-16 | 344 | 407 | 64 | + Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. |
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0016491 | oxidoreductase activity |
| GO:0050660 | flavin adenine dinucleotide binding |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI16966.1 | 0 | 1 | 416 | 407 | 774 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI16966.1 | 0 | 247 | 384 | 85 | 221 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002264336.1 | 0 | 1 | 414 | 131 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002329230.1 | 0 | 1 | 422 | 119 | 537 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002533924.1 | 0 | 1 | 422 | 131 | 546 | d-lactate dehydrogenase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3fw9_A | 0 | 1 | 410 | 98 | 495 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3fw7_A | 0 | 1 | 410 | 101 | 498 | A Chain A, Structure Of Berberine Bridge Enzyme, H104a Variant |
| PDB | 4ec3_A | 0 | 1 | 410 | 104 | 501 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 1 | 410 | 104 | 501 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2j_A | 0 | 1 | 410 | 123 | 520 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EL451713 | 297 | 115 | 411 | 0 |
| GO028240 | 276 | 134 | 409 | 0 |
| HO777438 | 420 | 2 | 411 | 0 |
| ES434378 | 276 | 39 | 314 | 0 |
| EC936189 | 298 | 16 | 311 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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