Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10012641 |
Family | AA7 |
Protein Properties | Length: 536 Molecular Weight: 59773.2 Isoelectric Point: 9.4093 |
Chromosome | Chromosome/Scaffold: 101 Start: 396763 End: 398370 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 69 | 529 | 0 |
NLRFNTSSASKPLVIVTPLTTSHVQSAVLCSKKHGLHLRIRGGGHDYEGLSYVALSPPNLPFFILDLINLSRVTVDVASNTAWMQGGATIGELYYQIGTR SKTLAFPAGVCPTVGVGGHFSGGGYGLLLRKFGLAADHIVDAQLVDEKGRVLNRASMGEDHFWAIRGGGGNTFGVVTAWKVNLVPVPQNVTVFTVTHTTD KNATIILDKWQRVADTLPDDLFIRVILDRSSANIGRARFNSLYLGTPNVLLPLLSRRFPELSATREDLVELSWIQSVLYFAGYPTNSSLEVLRSRVPLDP RRNFKAKSDYVLDPIPEHAVEGVWRRILRPKIEAPEVILSPYGGRMSEISESSIPFPHRAGNKFKIQHLIYWVKEGEKAKNRHIGWIRELYGYLAPHVSK NPRAAYVNYRDLDVGRNNGEEGDEDEQEEWGVKYFKGNYKRLVRVKTVVDPMNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 536 Download |
MMIINYLAAI LLLFSFSWND NIVLASSSSV HQNFIHCLST SSAANVSKIT FYTPSDPSYS 60 SVLQFSIQNL RFNTSSASKP LVIVTPLTTS HVQSAVLCSK KHGLHLRIRG GGHDYEGLSY 120 VALSPPNLPF FILDLINLSR VTVDVASNTA WMQGGATIGE LYYQIGTRSK TLAFPAGVCP 180 TVGVGGHFSG GGYGLLLRKF GLAADHIVDA QLVDEKGRVL NRASMGEDHF WAIRGGGGNT 240 FGVVTAWKVN LVPVPQNVTV FTVTHTTDKN ATIILDKWQR VADTLPDDLF IRVILDRSSA 300 NIGRARFNSL YLGTPNVLLP LLSRRFPELS ATREDLVELS WIQSVLYFAG YPTNSSLEVL 360 RSRVPLDPRR NFKAKSDYVL DPIPEHAVEG VWRRILRPKI EAPEVILSPY GGRMSEISES 420 SIPFPHRAGN KFKIQHLIYW VKEGEKAKNR HIGWIRELYG YLAPHVSKNP RAAYVNYRDL 480 DVGRNNGEEG DEDEQEEWGV KYFKGNYKRL VRVKTVVDPM NFFRNEQSIS PIYND* 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-9 | 80 | 532 | 470 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-10 | 80 | 221 | 144 | + 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 | 9.0e-16 | 473 | 529 | 57 | + 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. |
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 |
RefSeq | XP_002299020.1 | 0 | 26 | 532 | 23 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299022.1 | 0 | 26 | 532 | 16 | 523 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330608.1 | 0 | 25 | 532 | 24 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330609.1 | 0 | 26 | 532 | 23 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 26 | 532 | 16 | 524 | predicted protein [Populus trichocarpa] |
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 | 27 | 532 | 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 |
PDB | 4dns_A | 0 | 27 | 532 | 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 |
PDB | 3vte_A | 0 | 32 | 532 | 5 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 29 | 532 | 6 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 29 | 532 | 6 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |