Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma08g08570.2 |
Family | AA7 |
Protein Properties | Length: 594 Molecular Weight: 66576.2 Isoelectric Point: 10.1307 |
Chromosome | Chromosome/Scaffold: 08 Start: 6119504 End: 6121708 |
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 | 132 | 584 | 0 |
SVPKPDFIFTPLDDSQVQAAVVCAKKLGIHMRVRSGGHDYEGLSYVSLIEKPFMILDLAKLRAVNVDIARNTAWIQAGATIGEVYYRISEKSAVHGFPAG LCTTLGIGGHITGGAYGSMMRKYGLGADNVLDARIVDANGKVLDRKAMGEDLFWAIRGGGGGSFGVILWWKIKLVPVPQTVTVFTVTKTLEQGGSKLLHR WQQVAPHIDENLFIRVIIQPGNGTVPGKRTVTTSYNALFLGGANRLLQVMKHGFPELGLTRKDCVETSWIESVLYIAGYPDGTAPEVLLQGKSTTKAYFK AKSDFVREVITEKSLNALWKIFLQDDGPLMIWNPYGGKMSRIAESATPFPHRKGVLYKIQHVTGWLDGEKSMAKHMNWMRKFYFYMAPYVSKYPRETYVN YRDLDIGMNQKNNTSLLKASSWGYRYFKGNFNRLVKVKTKVDPSNFFRHEQSI |
Full Sequence |
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Protein Sequence Length: 594 Download |
MNQIKMKYPF TISHDVCLKS STRIIATLMK LALPSSNQCI YIQAKQTIYL NTRESRNQRT 60 MKSLRSILAT FVVLLSISLT ISLPIEEAFN HCLTQHSQTP NQFPSSIYTY TNGSFTSILE 120 STAQNLRYLL PSVPKPDFIF TPLDDSQVQA AVVCAKKLGI HMRVRSGGHD YEGLSYVSLI 180 EKPFMILDLA KLRAVNVDIA RNTAWIQAGA TIGEVYYRIS EKSAVHGFPA GLCTTLGIGG 240 HITGGAYGSM MRKYGLGADN VLDARIVDAN GKVLDRKAMG EDLFWAIRGG GGGSFGVILW 300 WKIKLVPVPQ TVTVFTVTKT LEQGGSKLLH RWQQVAPHID ENLFIRVIIQ PGNGTVPGKR 360 TVTTSYNALF LGGANRLLQV MKHGFPELGL TRKDCVETSW IESVLYIAGY PDGTAPEVLL 420 QGKSTTKAYF KAKSDFVREV ITEKSLNALW KIFLQDDGPL MIWNPYGGKM SRIAESATPF 480 PHRKGVLYKI QHVTGWLDGE KSMAKHMNWM RKFYFYMAPY VSKYPRETYV NYRDLDIGMN 540 QKNNTSLLKA SSWGYRYFKG NFNRLVKVKT KVDPSNFFRH EQSIPLLPTG KKE* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 0.008 | 136 | 298 | 166 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
COG0277 | GlcD | 7.0e-14 | 136 | 305 | 178 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 1.0e-18 | 528 | 585 | 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 | 4.0e-22 | 136 | 275 | 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 | |
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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 |
EMBL | CAN81654.1 | 0 | 73 | 588 | 14 | 528 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268361.1 | 0 | 66 | 588 | 7 | 528 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299030.1 | 0 | 82 | 588 | 1 | 507 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317089.1 | 0 | 84 | 593 | 26 | 535 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523164.1 | 0 | 82 | 589 | 26 | 533 | 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 | 4dns_B | 0 | 85 | 587 | 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 |
PDB | 4dns_A | 0 | 85 | 587 | 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 |
PDB | 3vte_A | 0 | 87 | 588 | 5 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 86 | 587 | 8 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 86 | 587 | 8 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |