| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000281703 |
| Family | AA7 |
| Protein Properties | Length: 240 Molecular Weight: 26518.2 Isoelectric Point: 7.9917 |
| Chromosome | Chromosome/Scaffold: 008389364 Start: 19915 End: 20736 |
| 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 | 9 | 135 | 0 |
| VRPFHESEIQAAVLCSKKLGLQVRVRSGGHDYEGPSYLCKTPFIIIDLINLRYIEVNLADETAWAQSGATLGELYYSIAKKSWVHGFSGGLCPTVGIGGH LSGGGFGILIRKHGLAADNVVDARFIA | |||
| Full Sequence |
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| Protein Sequence Length: 240 Download |
| MTPHLNSLVR PFHESEIQAA VLCSKKLGLQ VRVRSGGHDY EGPSYLCKTP FIIIDLINLR 60 YIEVNLADET AWAQSGATLG ELYYSIAKKS WVHGFSGGLC PTVGIGGHLS GGGFGILIRK 120 HGLAADNVVD ARFIAIQKSP LEDEFQSQIR LCEEPNTRTG TPRDLGEVSA GTKLHYKDLD 180 LGANKEDNTS FLVASAWRTR YFKGNFKRLA QVKSKVDPDN FFRNEQSIPP LPSLFPITEV 240 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 3.0e-7 | 8 | 134 | 128 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam08031 | BBE | 2.0e-15 | 176 | 229 | 54 | + 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 | 2.0e-18 | 8 | 134 | 128 | + 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 | ABC41951.1 | 0 | 8 | 134 | 79 | 205 | FAD-linked oxidoreductase 2 [Glycine max] |
| RefSeq | XP_002330615.1 | 0 | 3 | 144 | 81 | 220 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002330615.1 | 3e-16 | 174 | 231 | 475 | 532 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523167.1 | 0 | 8 | 144 | 76 | 212 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523167.1 | 5e-17 | 174 | 229 | 467 | 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 | 1e-36 | 2 | 142 | 51 | 191 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3vte_A | 0.000000000000008 | 174 | 232 | 455 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3fw9_A | 1e-32 | 6 | 134 | 47 | 175 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3fw9_A | 0.00001 | 174 | 231 | 432 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 4ec3_A | 1e-32 | 6 | 134 | 53 | 181 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BQ165732 | 135 | 8 | 142 | 0 |
| BW653574 | 127 | 8 | 134 | 0 |
| EG989592 | 135 | 8 | 142 | 0 |
| CF920811 | 174 | 8 | 160 | 0 |
| FF387975 | 127 | 8 | 134 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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