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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna20171.1-v1.0-hybrid |
Family | AA7 |
Protein Properties | Length: 509 Molecular Weight: 56974.1 Isoelectric Point: 7.6494 |
Chromosome | Chromosome/Scaffold: 3 Start: 8494867 End: 8496442 |
Description | FAD-binding Berberine family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 166 | 500 | 0 |
ISGGGIGTIFRKYGLASDNVIDARIVDVNGRILDRKSMGEELFWAIRGGGGSSFGVILAWKLRLVPVPPAVTVCHITKTKEQDATKLLLKWQNIADKLPE ELFIRLVIRSGDKTIIVEFGSLFLGPVEKLFHLMQDNFPELSLGRSHCTEMSWIQSVLDFAGYSIHESLEILLKRRQFSIIFKAKSDYVTEPISEAGLEG LWQRLVEANTSFMILTPYGGKMSEIADSETAFPHRRGNIYEIQYMVVWDDGKDTEKYVGFMRRLYAYMAPYVSKSPRAAYLNYRDLDLGRNNNGNTSYAQ ASIWGLKYFKNNFRKLVHVKTLVDPGNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 509 Download |
METSHAKLFP LLFILLNSAW SIASSSISES FVQCLSSHIQ NSNSSNEIIL TRTSSAYPSV 60 LDSSIQNLRF SNNSTPKPEA IITPFDESHV QAAVICSKKN GLQIRTRSGG HDYEGLSYVS 120 RAPFIIIDLF NLRSIDVDIE NESAWVKSGA TLGEGFVPPL VLGDDISGGG IGTIFRKYGL 180 ASDNVIDARI VDVNGRILDR KSMGEELFWA IRGGGGSSFG VILAWKLRLV PVPPAVTVCH 240 ITKTKEQDAT KLLLKWQNIA DKLPEELFIR LVIRSGDKTI IVEFGSLFLG PVEKLFHLMQ 300 DNFPELSLGR SHCTEMSWIQ SVLDFAGYSI HESLEILLKR RQFSIIFKAK SDYVTEPISE 360 AGLEGLWQRL VEANTSFMIL TPYGGKMSEI ADSETAFPHR RGNIYEIQYM VVWDDGKDTE 420 KYVGFMRRLY AYMAPYVSKS PRAAYLNYRD LDLGRNNNGN TSYAQASIWG LKYFKNNFRK 480 LVHVKTLVDP GNFFRNEQSI PVFSSDRK* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02805 | PLN02805 | 0.003 | 78 | 246 | 191 | + D-lactate dehydrogenase [cytochrome] | ||
pfam08031 | BBE | 1.0e-15 | 444 | 501 | 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 | 2.0e-17 | 78 | 501 | 457 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-17 | 78 | 199 | 139 | + 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 - 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 | 29 | 501 | 5 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 24 | 501 | 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 | 4dns_A | 0 | 24 | 501 | 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_B | 0 | 29 | 501 | 9 | 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 | 29 | 501 | 9 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |