| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 30075.m001137 |
| Family | AA7 |
| Protein Properties | Length: 442 Molecular Weight: 48943.8 Isoelectric Point: 6.2892 |
| Chromosome | Chromosome/Scaffold: 30075 Start: 53966 End: 55294 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 66 | 295 | 0 |
| NRRFNTSTTPKPLVIVTPLNVSHVQAAIICSKRHGMHIRVRSGGHDYEGLSYVSVHPFVIVDLINLQSITVDAANNTAWVQAGATIGNLYYSIAERSRTL AFPAGVCPTVGIGGHFTGGGYGMLLRKYGLAADNIIDAVLIDVNGRVLDRASMGEDLFWAIRGGGGNTFGIVISWKINLVPVPATVTVFTVEKTLEQNAT QLVNRWQYIADKLHEDLFIRVIIERVNSTS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 442 Download |
| MNSSSYILPV LVFSLLSFSW ATSAQTHEDF LECLHLQSQD STSISRIIYT PINSSYSSVL 60 QFSIQNRRFN TSTTPKPLVI VTPLNVSHVQ AAIICSKRHG MHIRVRSGGH DYEGLSYVSV 120 HPFVIVDLIN LQSITVDAAN NTAWVQAGAT IGNLYYSIAE RSRTLAFPAG VCPTVGIGGH 180 FTGGGYGMLL RKYGLAADNI IDAVLIDVNG RVLDRASMGE DLFWAIRGGG GNTFGIVISW 240 KINLVPVPAT VTVFTVEKTL EQNATQLVNR WQYIADKLHE DLFIRVIIER VNSTSQQGKT 300 TVRAAFNSLF LGGVDRLLPL MQESFPELGL VREDCIEMSW IESILYFAGF SNSPLDILLN 360 RTQPSVRNFK AKSDYVKEPM PETALEGIWE RLSEVDVGAG QLIFSPYGGR MSEISESSIP 420 FPHRAGNLYK IQHLAYWDEE GL 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 2.0e-15 | 77 | 244 | 175 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 5.0e-21 | 77 | 214 | 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. | ||
| 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_002332196.1 | 0 | 20 | 442 | 14 | 436 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002334045.1 | 0 | 20 | 440 | 21 | 439 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002337136.1 | 0 | 24 | 441 | 25 | 443 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523148.1 | 0 | 1 | 442 | 1 | 442 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523149.1 | 0 | 51 | 442 | 25 | 379 | 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 | 24 | 440 | 1 | 425 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_B | 0 | 28 | 441 | 9 | 408 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_A | 0 | 28 | 441 | 9 | 408 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsh_A | 0 | 28 | 441 | 9 | 408 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 4dns_B | 0 | 23 | 441 | 6 | 408 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
