Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna20166.1-v1.0-hybrid |
Family | AA7 |
Protein Properties | Length: 547 Molecular Weight: 61447.2 Isoelectric Point: 8.2649 |
Chromosome | Chromosome/Scaffold: 3 Start: 8472149 End: 8473789 |
Description | FAD-binding Berberine family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 78 | 534 | 0 |
NLRFTTPKTPTPSFIVTPTHVSHIQASILCSKIHNLQVRIRSGGHDYDGLSYISDVPFIIIDMFNLRSITVNIEEESAWVESGATLGEVYYRIAEQSKIH GYPAGVCPTVGVGGHLSGGGYGNMMRKHGLSVDNILDAQIVDVNGRLLDRESMGEDLFWAIRGGGGASFGVIVSWKIKLVQVPEVVTVFRVERTLEQGAT DIVHQWQHVGNTIDDDLFIRVVVMPVNRKTQRTVKAKFVALYLGNAEKLEALMGERFPRLGLKHEDYVEIGWIESVLYWSNYPIGTSADVLLERIPQSEK FLKKKSDYIQEPMSKASLEGLWNKMRELKKPVLTFNPYGGKMSKISELDTPFPHRAGNVYKIQYSVNWKEEGSEAEDKHLDLIRRLYKYMAPYVSKSPRC SYLNYRDVDLGTNGNGNVSYSEASVWGTNYFKGNFERLVQVKTAVDPGNFFRYEQSI |
Full Sequence |
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Protein Sequence Length: 547 Download |
MWRKPTPKVM STQTTSATLA VVTFLLLHAS MAALDSIQDT FLQCLSNLTQ SPSPSISSVT 60 YFPTDPSYTP ILHSYIRNLR FTTPKTPTPS FIVTPTHVSH IQASILCSKI HNLQVRIRSG 120 GHDYDGLSYI SDVPFIIIDM FNLRSITVNI EEESAWVESG ATLGEVYYRI AEQSKIHGYP 180 AGVCPTVGVG GHLSGGGYGN MMRKHGLSVD NILDAQIVDV NGRLLDRESM GEDLFWAIRG 240 GGGASFGVIV SWKIKLVQVP EVVTVFRVER TLEQGATDIV HQWQHVGNTI DDDLFIRVVV 300 MPVNRKTQRT VKAKFVALYL GNAEKLEALM GERFPRLGLK HEDYVEIGWI ESVLYWSNYP 360 IGTSADVLLE RIPQSEKFLK KKSDYIQEPM SKASLEGLWN KMRELKKPVL TFNPYGGKMS 420 KISELDTPFP HRAGNVYKIQ YSVNWKEEGS EAEDKHLDLI RRLYKYMAPY VSKSPRCSYL 480 NYRDVDLGTN GNGNVSYSEA SVWGTNYFKG NFERLVQVKT AVDPGNFFRY EQSIPPLTSW 540 NGKMVE* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
COG0277 | GlcD | 5.0e-13 | 89 | 537 | 481 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam08031 | BBE | 1.0e-18 | 478 | 535 | 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. |
pfam01565 | FAD_binding_4 | 3.0e-19 | 89 | 226 | 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 | |
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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 - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 4dns_B | 0 | 37 | 537 | 9 | 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 | 37 | 537 | 9 | 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 | 3vte_A | 0 | 38 | 537 | 4 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 36 | 537 | 6 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 36 | 537 | 6 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
Sequence Alignments (This image is cropped. Click for full image.) |
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