y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma06g47980.1 |
Family | AA7 |
Protein Properties | Length: 528 Molecular Weight: 59560.4 Isoelectric Point: 9.1012 |
Chromosome | Chromosome/Scaffold: 06 Start: 50332495 End: 50334337 |
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 | 70 | 519 | 0 |
SSRKPLLILTPFHESEIQAAILCSKELGLQIRIRSGGHDYEGLSYLCKAPFVMVDLINIRSIEINLDDETTWVQAGASIGELYYKISKASKVHGFPAGTC PSVGIGGHISGGGVGTMFRKHGLAADNVVDAYLIDANGKIHDRKSMGEDVFWAIRGGSATSFGVILAWKIRLVRVPPILTGFNIHRTLEEGASKLIHRWQ HIAHELHEDLFIRIVAQNSGDKSKTFQATFESLFLGGIDRLIPLMNASFPELGLQAEDCTEMSWIQSVLFFSGYNKGDSPEVLLNRTTTYKSSFKAKSDF VKEPIPKTGLEGIWKMLQEEETLALLLMEPYGGRMNEISESEIPFPHRKGNLYNIQYLVKWEVNSNEASKKHLHWAKRVYRYMTPYVSKSPRAAYFNYKD LDLGKNKHHNTSYSKASVWGKKYFKGNFRRLAQIKTKFDPQNFFSNEQSI |
Full Sequence |
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Protein Sequence Length: 528 Download |
MGYLAVFLTL LLSISCVDST LVEKKFTQCM LITRVDGNSE AIEKMLFRSS SSLYTQILES 60 LEQNPRWLNS SRKPLLILTP FHESEIQAAI LCSKELGLQI RIRSGGHDYE GLSYLCKAPF 120 VMVDLINIRS IEINLDDETT WVQAGASIGE LYYKISKASK VHGFPAGTCP SVGIGGHISG 180 GGVGTMFRKH GLAADNVVDA YLIDANGKIH DRKSMGEDVF WAIRGGSATS FGVILAWKIR 240 LVRVPPILTG FNIHRTLEEG ASKLIHRWQH IAHELHEDLF IRIVAQNSGD KSKTFQATFE 300 SLFLGGIDRL IPLMNASFPE LGLQAEDCTE MSWIQSVLFF SGYNKGDSPE VLLNRTTTYK 360 SSFKAKSDFV KEPIPKTGLE GIWKMLQEEE TLALLLMEPY GGRMNEISES EIPFPHRKGN 420 LYNIQYLVKW EVNSNEASKK HLHWAKRVYR YMTPYVSKSP RAAYFNYKDL DLGKNKHHNT 480 SYSKASVWGK KYFKGNFRRL AQIKTKFDPQ NFFSNEQSIP LLHTHPS* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 5.0e-17 | 72 | 522 | 477 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 2.0e-17 | 463 | 520 | 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. | ||
pfam01565 | FAD_binding_4 | 8.0e-18 | 74 | 211 | 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABC41950.1 | 0 | 1 | 527 | 3 | 528 | FAD-linked oxidoreductase 1 [Glycine max] |
GenBank | ABC41951.1 | 0 | 1 | 527 | 3 | 529 | FAD-linked oxidoreductase 2 [Glycine max] |
RefSeq | XP_002267029.1 | 0 | 4 | 522 | 251 | 770 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002330615.1 | 0 | 19 | 524 | 28 | 534 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523167.1 | 0 | 1 | 520 | 1 | 522 | Reticuline oxidase precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vte_A | 0 | 38 | 525 | 17 | 516 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 40 | 522 | 18 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 40 | 522 | 18 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsh_A | 0 | 40 | 522 | 18 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 4dns_B | 0 | 22 | 522 | 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 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |