| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_004967m |
| Family | AA7 |
| Protein Properties | Length: 547 Molecular Weight: 61369.8 Isoelectric Point: 9.4567 |
| Chromosome | Chromosome/Scaffold: 07478 Start: 823779 End: 825446 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 74 | 299 | 0 |
| SVPKPEFIFTPLHETHIQAAVICSKQLGIHLRVRSGGHDYEGLSYTSEIETPFIIVDLSKLRSVTVDIEDNSAWVQAGATIGEAYYRIAEKSKIHGFPAG LCSSLGVGGHITGGAYGSMMRKYGLGADNVIDARIIDVNGRVLNRQAMGEDLFWAIRGGGGASFGIIVSWKLKLVPVPATVTVFTVTKTLEQNATEILYR WQQVADKLDEDLFIRVIIQPATVGNS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 547 Download |
| MVPSISSIFS ILVILVLSPS FSLSLLIRDS FLQCLNVNTE TVIPYSTAFF TPDNSSFSSI 60 LQSSAQNLRY LLPSVPKPEF IFTPLHETHI QAAVICSKQL GIHLRVRSGG HDYEGLSYTS 120 EIETPFIIVD LSKLRSVTVD IEDNSAWVQA GATIGEAYYR IAEKSKIHGF PAGLCSSLGV 180 GGHITGGAYG SMMRKYGLGA DNVIDARIID VNGRVLNRQA MGEDLFWAIR GGGGASFGII 240 VSWKLKLVPV PATVTVFTVT KTLEQNATEI LYRWQQVADK LDEDLFIRVI IQPATVGNST 300 TRTITTSYNA LFLGDANRLL HVMEKSFPEL GLTRKDCIET SWIKSVLYIA GYPSTTPPEI 360 LLQGKSLFKN YFKAKSDFVK EPIPETGLKG LWKRLLNEDI PLMIWNPYGG MMSKISEYEI 420 PFPHRKGNSF MIQYLSIWQD GEKSAAKHMK WIRKLYNYMA PYVSMFPRSA YVNYRDLDLG 480 KNKKMNTSFI EATAWGNKYF NDNFNRLVEV KTKVDPDNFF RHEQSIPPLP VSMWKRRARG 540 GEGVRV* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02805 | PLN02805 | 0.001 | 78 | 247 | 179 | + D-lactate dehydrogenase [cytochrome] | ||
| TIGR01678 | FAD_lactone_ox | 0.001 | 77 | 242 | 171 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
| pfam08031 | BBE | 1.0e-18 | 470 | 527 | 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 | 4.0e-23 | 90 | 529 | 459 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-27 | 78 | 217 | 141 | + 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 |
| EMBL | CAN81654.1 | 0 | 12 | 530 | 11 | 528 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002268361.1 | 0 | 1 | 530 | 1 | 528 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299030.1 | 0 | 24 | 530 | 1 | 507 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523162.1 | 0 | 21 | 533 | 23 | 535 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 0 | 21 | 533 | 23 | 535 | 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 | 28 | 530 | 4 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 27 | 529 | 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 | 27 | 529 | 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 | 3tsj_B | 0 | 28 | 529 | 8 | 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 | 28 | 529 | 8 | 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 |
