| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.model.supercontig_166.49 |
| Family | AA7 |
| Protein Properties | Length: 507 Molecular Weight: 57622.3 Isoelectric Point: 8.8288 |
| Chromosome | Chromosome/Scaffold: 166 Start: 444134 End: 445654 |
| 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 | 39 | 258 | 0 |
| PRWVNSTASKPLLVMTPFHESEIQAAIICSRRYDLQIRIRSGGHDYEGLSYLCATPFILIDLVNLRSITVNIEDETAWVQSGATLGELYYAIAKRSGIHG FPAGLCSTVGIGGHLTGGGFGTMVRKYGLAADNILDAYLIDVNGRVMNRETMGEELFWAIRGGGGASFGIILSWKIKLVPVPKTVTAFTVSRTLEEGATK LVHRWQYIAHKMHEDLFIRI | |||
| Full Sequence |
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| Protein Sequence Length: 507 Download |
| MFVPCMSTYF GAYTKNMEIM HTPNSSLYSY ILQSSMQNPR WVNSTASKPL LVMTPFHESE 60 IQAAIICSRR YDLQIRIRSG GHDYEGLSYL CATPFILIDL VNLRSITVNI EDETAWVQSG 120 ATLGELYYAI AKRSGIHGFP AGLCSTVGIG GHLTGGGFGT MVRKYGLAAD NILDAYLIDV 180 NGRVMNRETM GEELFWAIRG GGGASFGIIL SWKIKLVPVP KTVTAFTVSR TLEEGATKLV 240 HRWQYIAHKM HEDLFIRIII QNVCTSNKRT VQASFDSLFL GGIDRLIPLM SAIFPELGLK 300 PKDCNEMSWV ESALYFAEFK KGQPLEVLLG RTLLSKSNFK AKSDFVQEPI PEYGLEGIWE 360 RFLEEDLPMM IMDPFGGRMD QISESDVPFP HREGNLYNIQ YLVRWEDNRI EESNRHKNWI 420 RMLYRYMKPF VSKSPRAAYF NFRDLDLGIN NHTKTSYSEG RVWGLKYFKG NFRRLAQVKS 480 NVDPDNFFRS AQSIPPLPAP RKLQNQ* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 2.0e-15 | 438 | 495 | 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. | ||
| COG0277 | GlcD | 2.0e-21 | 49 | 497 | 464 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 7.0e-22 | 49 | 184 | 137 | + 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 |
| GenBank | ABC41950.1 | 0 | 2 | 497 | 28 | 523 | FAD-linked oxidoreductase 1 [Glycine max] |
| GenBank | ABC41951.1 | 0 | 2 | 497 | 28 | 524 | FAD-linked oxidoreductase 2 [Glycine max] |
| RefSeq | XP_002267029.1 | 0 | 2 | 498 | 272 | 771 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002330615.1 | 0 | 2 | 497 | 35 | 532 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523167.1 | 0 | 2 | 495 | 26 | 522 | 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 | 2 | 498 | 7 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 20 | 497 | 26 | 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 | 20 | 497 | 26 | 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 | 9 | 497 | 11 | 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 | 9 | 497 | 11 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO777438 | 505 | 2 | 497 | 0 |
| CV529433 | 311 | 37 | 346 | 0 |
| EG029578 | 314 | 161 | 471 | 0 |
| HO798639 | 323 | 24 | 340 | 0 |
| FE675676 | 284 | 66 | 349 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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