| Basic Information | |
|---|---|
| Species | Carica papaya |
| Cazyme ID | evm.model.supercontig_677.5 |
| Family | AA7 |
| Protein Properties | Length: 531 Molecular Weight: 59638.4 Isoelectric Point: 8.4095 |
| Chromosome | Chromosome/Scaffold: 677 Start: 14023 End: 15615 |
| 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 | 66 | 523 | 0 |
| NARFNTSSAPKPIIIITPLEESHVRAAVICTKKVGFILKIRSGGHDYDGISYVSDSPFFILDMYNLRTVTVDMEEESAWVGAGATLGEVYHAIWTKSKVH GFPAGVCPTVGAGGHISGGGYGNILRKHGLSVDHMVDAKIVDVNGRILDRESMGEDLFWAIRGGGGASFGVILSYKIKLVPVPETVTVFRLEYLMDQNAL DITHKWQFVAPKTDPNLFMRVLIQPVTRNKKRTIRTTIITLFLGKADEVVSLLGKEFPEMGLKKENCTEMTWVQSVLWWANFDNVTEISPDVLLDRNLDS ANFLKRKSDYVGKEIGKSDLESLFKQMIKIGKVGLVFNPYGGRMREFSSTETPFPHREKLYKIQYSVNWEEPGNDADKQFMNEIRTLYGFMTPLVSQNPR SSYLNYRDLDIGTNTNGGKIFEEGEVYGRKYFGDNFDRLVKVKTAVDPGNFFWNEQSI | |||
| Full Sequence |
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| Protein Sequence Length: 531 Download |
| MAKPIDFIPL CLLLFTLLHS SSANEDSVHK SFLNCMIKET NPEISNTIFA KTNSSYTSVL 60 RAYIRNARFN TSSAPKPIII ITPLEESHVR AAVICTKKVG FILKIRSGGH DYDGISYVSD 120 SPFFILDMYN LRTVTVDMEE ESAWVGAGAT LGEVYHAIWT KSKVHGFPAG VCPTVGAGGH 180 ISGGGYGNIL RKHGLSVDHM VDAKIVDVNG RILDRESMGE DLFWAIRGGG GASFGVILSY 240 KIKLVPVPET VTVFRLEYLM DQNALDITHK WQFVAPKTDP NLFMRVLIQP VTRNKKRTIR 300 TTIITLFLGK ADEVVSLLGK EFPEMGLKKE NCTEMTWVQS VLWWANFDNV TEISPDVLLD 360 RNLDSANFLK RKSDYVGKEI GKSDLESLFK QMIKIGKVGL VFNPYGGRMR EFSSTETPFP 420 HREKLYKIQY SVNWEEPGND ADKQFMNEIR TLYGFMTPLV SQNPRSSYLN YRDLDIGTNT 480 NGGKIFEEGE VYGRKYFGDN FDRLVKVKTA VDPGNFFWNE QSIPPHKSKA * 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 4.0e-13 | 58 | 525 | 493 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 7.0e-14 | 77 | 214 | 143 | + 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-18 | 467 | 524 | 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. | ||
| 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 | NP_193816.1 | 0 | 28 | 530 | 34 | 539 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | XP_002299028.1 | 0 | 1 | 530 | 1 | 536 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317087.1 | 0 | 20 | 530 | 24 | 535 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523157.1 | 0 | 24 | 530 | 32 | 539 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523158.1 | 0 | 1 | 530 | 1 | 539 | 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 | 30 | 525 | 5 | 512 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 27 | 525 | 8 | 495 | 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 | 27 | 525 | 8 | 495 | 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 | 27 | 525 | 6 | 495 | 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 | 27 | 525 | 6 | 495 | 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 |
| EX265342 | 265 | 267 | 531 | 0 |
| EX268001 | 301 | 232 | 527 | 0 |
| EX255739 | 280 | 135 | 414 | 0 |
| EX274550 | 224 | 308 | 531 | 0 |
| EX268001 | 42 | 490 | 531 | 0.0000000002 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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