| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.TU.contig_36442.2 |
| Family | AA7 |
| Protein Properties | Length: 444 Molecular Weight: 49800 Isoelectric Point: 8.2555 |
| Chromosome | Chromosome/Scaffold: 36442 Start: 1485 End: 2816 |
| 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 | 437 | 0 |
| DKSHVRATILCSKAGGLQMRIRSGGHDYDGLSYVSDVPFVLLDMFNLRSIDIDLKDESAWVQSGATVGELYYRIAEKSNVRGFPAGICPTLGVGGHFSGG GYGNMMRKYGLSVDNVVDAEVVDVNGNVLDRKGMGEDLFWAIRGGGAASFCVVLSWKIKLVPVPEKVTVFQVEKTMEEGAVDLVVKWQEVADKLDENLFI RLMLSPTKISTKNSVKASFVAMFLGQSNSLLSLMNHSFPELGLQQKDCIEMKWIESVPFWTGSPNGTQIDDLLIRESKRPVFLKRKSDYVQKPISKAAIE SIFKAIIESEYVGMLWNPYGGKMSEISESETPFPHRAGNKFKIQYSVNWNEEGNDIVNKYLDRTRRLFGAMTPFVSKNPREAFLNYRDIDIGGNLNGTYD EGKVYGIKYFKNNFDRLVQVKNKVDPENFFRYEQSI | |||
| Full Sequence |
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| Protein Sequence Length: 444 Download |
| MDKSHVRATI LCSKAGGLQM RIRSGGHDYD GLSYVSDVPF VLLDMFNLRS IDIDLKDESA 60 WVQSGATVGE LYYRIAEKSN VRGFPAGICP TLGVGGHFSG GGYGNMMRKY GLSVDNVVDA 120 EVVDVNGNVL DRKGMGEDLF WAIRGGGAAS FCVVLSWKIK LVPVPEKVTV FQVEKTMEEG 180 AVDLVVKWQE VADKLDENLF IRLMLSPTKI STKNSVKASF VAMFLGQSNS LLSLMNHSFP 240 ELGLQQKDCI EMKWIESVPF WTGSPNGTQI DDLLIRESKR PVFLKRKSDY VQKPISKAAI 300 ESIFKAIIES EYVGMLWNPY GGKMSEISES ETPFPHRAGN KFKIQYSVNW NEEGNDIVNK 360 YLDRTRRLFG AMTPFVSKNP REAFLNYRDI DIGGNLNGTY DEGKVYGIKY FKNNFDRLVQ 420 VKNKVDPENF FRYEQSIPTK NKA* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 0.002 | 6 | 440 | 466 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-9 | 2 | 112 | 112 | + 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 | 9.0e-17 | 383 | 438 | 56 | + 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 |
| GenBank | AAF79255.1 | 0 | 4 | 438 | 88 | 522 | AC023279_4 F12K21.9 [Arabidopsis thaliana] |
| RefSeq | NP_564449.1 | 0 | 4 | 438 | 88 | 522 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | XP_002317086.1 | 0 | 3 | 443 | 83 | 529 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523152.1 | 0 | 1 | 439 | 66 | 507 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523155.1 | 0 | 4 | 440 | 86 | 524 | 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 | 4dns_B | 0 | 2 | 438 | 63 | 494 | 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 | 2 | 438 | 63 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3vte_A | 0 | 2 | 438 | 62 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_B | 0 | 4 | 438 | 63 | 494 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_A | 0 | 4 | 438 | 63 | 494 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| 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 | 449 | 1 | 438 | 0 |
| DY290183 | 364 | 26 | 387 | 0 |
| DY262774 | 379 | 61 | 432 | 0 |
| DY293389 | 390 | 60 | 438 | 0 |
| FC896393 | 306 | 135 | 438 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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