| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01021739001 |
| Family | AA7 |
| Protein Properties | Length: 431 Molecular Weight: 47918.7 Isoelectric Point: 8.8853 |
| Chromosome | Chromosome/Scaffold: 10 Start: 10359501 End: 10361096 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA7 | 68 | 188 | 7.59504e-43 |
| NLRFNTSTTPKPRLIITATHESHIQAAIICSKKHGLQMKIRSGGHDFEGVSYVSDVPFFILDMFNLRSISVDIEDESAWVQAGATLGEMYYRIAEKSKTH GFPAGVCPTVGAGGHFSGGGY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 431 Download |
| MGTSSSSMLS LLSIILLLSL SWAASDSVHG AFLQCLSTHS QSSHPISAAL YTPDNSSYSS 60 VLESYIRNLR FNTSTTPKPR LIITATHESH IQAAIICSKK HGLQMKIRSG GHDFEGVSYV 120 SDVPFFILDM FNLRSISVDI EDESAWVQAG ATLGEMYYRI AEKSKTHGFP AGVCPTVGAG 180 GHFSGGGYDL FWAIIAGGGA SYGVIVSYKI KLVQVPATVT VFRVARTLEQ NATNIVYQWQ 240 QVADKVDGDL FIRLTMDALL DRNPQVLTHL KRKSDYLKEP IPKAGLEGIW KKMIELQTPY 300 LVFNPYGGKM AEISPSATPF PHRAGNLCKI MYATNWDEEG SEAAERYINL TQKLYSYMTP 360 FVSKSPREAF LNYRDLDLGV NHNGKNSYLE GRIYGIKYFK ENFNRLVRIK TKVDPGNFFR 420 NEQSIPTLPY * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 2.0e-8 | 60 | 263 | 248 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam08031 | BBE | 2.0e-17 | 369 | 426 | 58 | + 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. | ||
| pfam01565 | FAD_binding_4 | 7.0e-18 | 79 | 208 | 131 | + 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. | ||
| 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 | CAN60572.1 | 0 | 1 | 430 | 1 | 531 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN80091.1 | 0 | 1 | 430 | 1 | 531 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI31076.1 | 0 | 1 | 430 | 1 | 430 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002269462.1 | 0 | 1 | 430 | 1 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002270585.1 | 0 | 1 | 430 | 1 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4dns_B | 0 | 25 | 428 | 6 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 4dns_A | 0 | 25 | 428 | 6 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_B | 0 | 50 | 428 | 24 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_A | 0 | 50 | 428 | 24 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsh_A | 0 | 50 | 428 | 24 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| dehydroscoulerine biosynthesis | RXN-10888 | EC-1.21.3 | reticuline oxidase |
| sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
