| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01037107001 |
| Family | AA7 |
| Protein Properties | Length: 791 Molecular Weight: 87500.8 Isoelectric Point: 4.8573 |
| Chromosome | Chromosome/Scaffold: 18 Start: 29086519 End: 29097009 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 342 | 533 | 0 |
| NLRYAVPTAPKPVAIAIPQSLKQLVNSMRCCREGWYEFRVRCGGHSYEGISSVVPDGNPFVIIDMMSLNQVSVDVESETAWVEGGATLGETYYAVAEASN VHGFSAGSCPTVGVGGHIAGGGFGLLSRKYGLAADNVVDALLIDADGRVLDRKAMGEDVFWAIRGGGGGDWGIVYAWKIKLLKVPETVTSFD | |||
| Full Sequence |
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| Protein Sequence Length: 791 Download |
| MSLNQVLVDL ESETAWVEGG ATLGETYYAV AEASNVHGFS AGSCPTVGVG GHISGGGFGL 60 LSRKYGLAAD NVVDALLIDA DGRLAKSDYV RTPISMKGLR TALDTLEKEP KGYVILDPYG 120 GEMERIGSDA IAFPHRKGNL FAIQYMVAWE EDSLMSYKYI DWIRGFYKSM TPHVSWGPRA 180 AYVNYMDLDL GVMEMVNSSF SSGDPVEIAR AWGEKYFLNN YESVFDNLML YIGWPCAFIS 240 PCFCPQLLIL YVINLGVKSH LLSIVSTSIS IRRSIAMVKY LGNPHSLFII TFIAFVVPCF 300 CDPTDIISSC LIRHNVYNFT LLPHNGSQSP DYYRLLNFSL QNLRYAVPTA PKPVAIAIPQ 360 SLKQLVNSMR CCREGWYEFR VRCGGHSYEG ISSVVPDGNP FVIIDMMSLN QVSVDVESET 420 AWVEGGATLG ETYYAVAEAS NVHGFSAGSC PTVGVGGHIA GGGFGLLSRK YGLAADNVVD 480 ALLIDADGRV LDRKAMGEDV FWAIRGGGGG DWGIVYAWKI KLLKVPETVT SFDEETGVSA 540 SFKGFYLGSR NEAMSILNRV FPELGVEKED CREMSWIESI LYFSGLPNGS SISELRNRYL 600 EDKLYFKAKS DYVRTPISME GLVTALDILE MEPKGSVVLD PYGGEMEKIS SDALPFPHRK 660 GNLFSIQYMV AWEEDSTAMS NKYIDWIRGF YKWMMPYVSQ GPRAAYVNYM DLDLGQMNSS 720 ISSNDPVEAA RDWGEKYFLN NYDRLVKVKT CIDPDNVFNN QQGIPPMPTA RLNNRSEGLG 780 VSERCMVVSY * 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01565 | FAD_binding_4 | 6.0e-9 | 3 | 84 | 83 | + 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. | ||
| COG0277 | GlcD | 7.0e-15 | 353 | 530 | 185 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam08031 | BBE | 2.0e-16 | 705 | 765 | 61 | + 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 | 4.0e-22 | 353 | 492 | 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 | CBI16966.1 | 0 | 1 | 790 | 1 | 790 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002264336.1 | 3e-32 | 1 | 88 | 131 | 218 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002264336.1 | 0 | 85 | 224 | 373 | 512 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002264336.1 | 0 | 277 | 770 | 1 | 537 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002329230.1 | 0 | 294 | 777 | 4 | 536 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3fw9_A | 0 | 309 | 767 | 4 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3fw9_A | 1e-28 | 76 | 224 | 324 | 472 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3fw9_A | 8e-23 | 1 | 84 | 98 | 181 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3d2j_A | 0 | 287 | 767 | 8 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3d2j_A | 2e-28 | 76 | 224 | 349 | 497 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FC883009 | 241 | 297 | 532 | 0 |
| EL451713 | 237 | 534 | 767 | 0 |
| DY275245 | 241 | 297 | 532 | 0 |
| EL451713 | 141 | 85 | 224 | 1.4013e-45 |
| FC883009 | 83 | 2 | 84 | 5e-27 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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