| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 30075.m001138 |
| Family | AA7 |
| Protein Properties | Length: 469 Molecular Weight: 52581.2 Isoelectric Point: 8.8432 |
| Chromosome | Chromosome/Scaffold: 30075 Start: 62894 End: 64409 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 41 | 463 | 0 |
| QATICSKRYGMHIRVRSGGHDYEGLSYVSALPFFIIDLINLQSVTVDAAKNTAWVQAGATIGKLYYSVCPTVGIGGHFSGGGYGMLLRKYGLAADNIIDA VLIDVNGRVLDRASMGEDLFWAIRGGGGNTFGIVISWKINLVPVPATVTVFTVEKTLKQNATQLVNGWQYIAEKLHEDLFIRVIIERVNSTSQQGKTTVR AAFNSLFLGGVDRLLPLMQESFPELGLVREDCINMSWIESILYFAGFSNSPLDILLSRTQPSVRNFKAKSDYVKEPMPETALEGIWERLSEMDVGAGQLI FSPYGGRMSEISESSIPFPHRAGNLYKIQHLAYWDEEGIVATRKHISWIRRLYSFLAPYVSKNPRAAYINYRDLDIGINNLGNTSYKQASIWGIKYFKIN FDRLVHVKTTVDPANFFRNEQSI | |||
| Full Sequence |
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| Protein Sequence Length: 469 Download |
| MKIFLNVFTF NLKTPLPSPE SYTPPINSSY SSVEQFSIQN QATICSKRYG MHIRVRSGGH 60 DYEGLSYVSA LPFFIIDLIN LQSVTVDAAK NTAWVQAGAT IGKLYYSVCP TVGIGGHFSG 120 GGYGMLLRKY GLAADNIIDA VLIDVNGRVL DRASMGEDLF WAIRGGGGNT FGIVISWKIN 180 LVPVPATVTV FTVEKTLKQN ATQLVNGWQY IAEKLHEDLF IRVIIERVNS TSQQGKTTVR 240 AAFNSLFLGG VDRLLPLMQE SFPELGLVRE DCINMSWIES ILYFAGFSNS PLDILLSRTQ 300 PSVRNFKAKS DYVKEPMPET ALEGIWERLS EMDVGAGQLI FSPYGGRMSE ISESSIPFPH 360 RAGNLYKIQH LAYWDEEGIV ATRKHISWIR RLYSFLAPYV SKNPRAAYIN YRDLDIGINN 420 LGNTSYKQAS IWGIKYFKIN FDRLVHVKTT VDPANFFRNE QSIQPLSSW 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 1.0e-8 | 48 | 181 | 157 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 3.0e-10 | 45 | 151 | 121 | + 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-15 | 407 | 463 | 57 | + 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 |
| RefSeq | XP_002299020.1 | 0 | 25 | 469 | 50 | 533 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002299022.1 | 0 | 25 | 469 | 43 | 526 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002332196.1 | 0 | 25 | 469 | 43 | 527 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523148.1 | 0 | 25 | 379 | 51 | 442 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523149.1 | 0 | 1 | 469 | 1 | 469 | Reticuline oxidase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 17 | 466 | 52 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 42 | 466 | 70 | 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 | 42 | 466 | 70 | 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 | 35 | 466 | 61 | 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 | 35 | 466 | 61 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO777438 | 483 | 27 | 467 | 0 |
| BQ516692 | 273 | 138 | 405 | 0 |
| DC894588 | 349 | 133 | 466 | 0 |
| AM731099 | 265 | 208 | 466 | 0 |
| DY262774 | 381 | 94 | 458 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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