| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma06g48000.1 |
| Family | AA7 |
| Protein Properties | Length: 530 Molecular Weight: 59900.8 Isoelectric Point: 7.9637 |
| Chromosome | Chromosome/Scaffold: 06 Start: 50348918 End: 50350863 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 66 | 290 | 0 |
| PRWVNISSRKPLMILTPFHESEIQAAILCSKELKLQLRVRSGGHDYEGLSYLSDVPFVMVDLINIRSIEINLADETAWVQAGASIGELYYKISKASKVHG FPAGTCPSVGIGGHISGGGQGLMLRKHGLAADNVVDAYLIDANGKIHDRKSMGEDVFWAIRGGDASSFGVILAWKIKLVRVPPIVTGFNVPRTPEEGVTD LIHRWQYIAHDLHEDLVIRVIAQIS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 530 Download |
| MELSYCAVFL ILLIPISRAD ATSVEKQFKE CLLTQLDGNS EHIEKITFTS SSTLYPQVWD 60 SLAQNPRWVN ISSRKPLMIL TPFHESEIQA AILCSKELKL QLRVRSGGHD YEGLSYLSDV 120 PFVMVDLINI RSIEINLADE TAWVQAGASI GELYYKISKA SKVHGFPAGT CPSVGIGGHI 180 SGGGQGLMLR KHGLAADNVV DAYLIDANGK IHDRKSMGED VFWAIRGGDA SSFGVILAWK 240 IKLVRVPPIV TGFNVPRTPE EGVTDLIHRW QYIAHDLHED LVIRVIAQIS GHDKSKKFRA 300 TFNSIFLGGV DRLIPLMNES FPELGLQAKD CTEMSWIQSV MFIAGYNIED PLELLLNRTT 360 MFKRSFKAKS DFFKEPVPKS GLEGAWKLLL EEEIAFLIME PYGGRMNEIS ESEIPFPHRK 420 GNLYNLQYLV NWEVNSDEAS RRHLQWAKMV YKYMTPYVSK SPRAAYFNYK DLDLGKNKLD 480 STSYSEASVW GKKYFKGNFR RLAQIKTKFD PLNFFRNEQS IPLLNSHHS* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 5.0e-18 | 465 | 522 | 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 | 1.0e-18 | 44 | 524 | 504 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 4.0e-19 | 76 | 213 | 140 | + 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 | ABC41950.1 | 0 | 1 | 529 | 1 | 528 | FAD-linked oxidoreductase 1 [Glycine max] |
| GenBank | ABC41951.1 | 0 | 1 | 529 | 1 | 529 | FAD-linked oxidoreductase 2 [Glycine max] |
| RefSeq | XP_002267029.1 | 0 | 7 | 524 | 252 | 770 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002330615.1 | 0 | 21 | 526 | 28 | 534 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523167.1 | 0 | 8 | 522 | 6 | 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 | 0 | 26 | 528 | 5 | 517 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_B | 0 | 23 | 524 | 6 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_A | 0 | 23 | 524 | 6 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsh_A | 0 | 23 | 524 | 6 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 4dns_B | 0 | 21 | 524 | 6 | 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 |
