Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10023375 |
Family | AA7 |
Protein Properties | Length: 538 Molecular Weight: 60204.8 Isoelectric Point: 8.4186 |
Chromosome | Chromosome/Scaffold: 98 Start: 769673 End: 771286 |
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 | 78 | 531 | 0 |
NSTSSTKPFLILTALDVSHVQTAVVCASKHNVQMKIRSGGHDYEALSYVSLTQQPFFILDMFSLRDVDVDIPSETAWIQTGAILGEVYYRIAEKSKVHGF PAGVCPTVGVGGHVSGAGYGNMLRKHGLTVDNVVDAALVDVNGRLLDRKSMGEDLFWAIRGGGGASFGVVISYKVNLVRVPELVTAFSVFKTVDEENGID IVDKWQHVADKLDERLFIRLVLNVVNATKVRARFLGFFLGDSAQLMSIMKEKFPELGLAQSDCIETSWIRSVLFWTDLPVETRPEVLLRRTTTTTRLKRK SDYVQRVIPREGLERLMKKMVELQVVGMVFNPYGGRMSEIAADATPFPHRAGNLWKIQYQANWNLAGEETEERNLEMVRRMYEFMTPFVSKKPRGAFLNY RDIDLGVNHNNGAGSYDEARSGYGVQYFRGNFKRLVEIKSKVDPGNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 538 Download |
MSFTTISFIL SITLLSITPT SLCHTSSESN FMQCLHNNSN PSNPISQAIY TPNDTASYSS 60 VLQAYIQNQR FNFINTTNST SSTKPFLILT ALDVSHVQTA VVCASKHNVQ MKIRSGGHDY 120 EALSYVSLTQ QPFFILDMFS LRDVDVDIPS ETAWIQTGAI LGEVYYRIAE KSKVHGFPAG 180 VCPTVGVGGH VSGAGYGNML RKHGLTVDNV VDAALVDVNG RLLDRKSMGE DLFWAIRGGG 240 GASFGVVISY KVNLVRVPEL VTAFSVFKTV DEENGIDIVD KWQHVADKLD ERLFIRLVLN 300 VVNATKVRAR FLGFFLGDSA QLMSIMKEKF PELGLAQSDC IETSWIRSVL FWTDLPVETR 360 PEVLLRRTTT TTRLKRKSDY VQRVIPREGL ERLMKKMVEL QVVGMVFNPY GGRMSEIAAD 420 ATPFPHRAGN LWKIQYQANW NLAGEETEER NLEMVRRMYE FMTPFVSKKP RGAFLNYRDI 480 DLGVNHNNGA GSYDEARSGY GVQYFRGNFK RLVEIKSKVD PGNFFRNEQS IPVAPSY* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-5 | 85 | 532 | 474 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-9 | 85 | 224 | 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. | ||
pfam08031 | BBE | 1.0e-15 | 473 | 532 | 60 | + 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 |
EMBL | CAN80091.1 | 0 | 31 | 535 | 32 | 530 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002269462.1 | 0 | 31 | 535 | 32 | 530 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002333959.1 | 0 | 11 | 535 | 13 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523151.1 | 0 | 19 | 537 | 25 | 539 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523152.1 | 0 | 26 | 537 | 7 | 511 | 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 | 30 | 537 | 6 | 516 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 28 | 532 | 10 | 494 | 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 | 28 | 532 | 10 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_B | 0 | 26 | 532 | 6 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_A | 0 | 26 | 532 | 6 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |