| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma15g14090.2 |
| Family | AA7 |
| Protein Properties | Length: 493 Molecular Weight: 54848.5 Isoelectric Point: 10.2343 |
| Chromosome | Chromosome/Scaffold: 15 Start: 10629110 End: 10635521 |
| 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 | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA7 | 112 | 247 | 0 |
| LGGIIVNVKNEVAMVQAGATLGEVYYRIWEKSKVLGFPAGVCPTVDVGGHISGGGYDNMLRKHGLSVDNVIDAQIVDVKGNLLNRKTMGEDLFWAIRGGG GASFGVILSFTFKLVPVPKTVTVFRVEKTLEENATD | |||
| Full Sequence |
|---|
| Protein Sequence Length: 493 Download |
| MAKPSLAYLF AAFLLLIVSI SLSKPSPKSS LYDTFLHCFT QHTNSSTQFS NIVFPQSNPK 60 FPFVTQNYIR NARFNTPLTQ KLLLIVTPQV ESHVQATVIC AKSVNSQPNI NLGGIIVNVK 120 NEVAMVQAGA TLGEVYYRIW EKSKVLGFPA GVCPTVDVGG HISGGGYDNM LRKHGLSVDN 180 VIDAQIVDVK GNLLNRKTMG EDLFWAIRGG GGASFGVILS FTFKLVPVPK TVTVFRVEKT 240 LEENATDFVL LFMRLLLQPV SSKVVKGGNT IRASVVALFL GGANEVVPIL AKQFPLLGLR 300 KENCTEVSWM DSVLWWDDDK SLKNGAKPET LLDRHANTAD FLKRKSDYVQ KAIPREGLEF 360 IWKRMIELGK TGLVFNPYGR KMAQGNLFKV QYSVTWKDPS LAAAQNFLNQ ARKLYSYMTP 420 FVSKNPRSAF LNYRDLDIGV NNFRKNSFQE GEVYGAKYFN GNFQRLIKVK TVVDSTNFFR 480 NEQSIPLAPS KA* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02441 | PLN02441 | 0.008 | 158 | 237 | 81 | + cytokinin dehydrogenase | ||
| pfam01565 | FAD_binding_4 | 2.0e-12 | 83 | 195 | 137 | + 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. | ||
| pfam08031 | BBE | 1.0e-13 | 429 | 486 | 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 | 3.0e-16 | 62 | 488 | 468 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| 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 |
| RefSeq | XP_002267223.1 | 0 | 30 | 486 | 33 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299028.1 | 0 | 1 | 492 | 1 | 536 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317087.1 | 0 | 1 | 492 | 1 | 535 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523157.1 | 0 | 29 | 492 | 34 | 539 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523158.1 | 0 | 29 | 492 | 34 | 539 | 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 | 33 | 489 | 5 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_B | 0 | 27 | 486 | 3 | 494 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_A | 0 | 27 | 486 | 3 | 494 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsh_A | 0 | 27 | 486 | 3 | 494 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 4dns_B | 0 | 35 | 486 | 13 | 494 | 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 |
| Transmembrane Domains | |
|---|---|
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| Start | End |
| 5 | 22 |
