y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 473304 |
Family | AA7 |
Protein Properties | Length: 527 Molecular Weight: 58705.7 Isoelectric Point: 9.4585 |
Chromosome | Chromosome/Scaffold: 1 Start: 13835182 End: 13836762 |
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 | 66 | 522 | 0 |
LRFDKPTTPKPIAIITPTTWSHISPALACARLLPVQVRIRSGGHDFEGLSYTSTAPFFVIDLLNFKSVDVNLTEGTAWVDTGATIGELYYKIAEKSNVLG FPAGLCTTLGVGGHISGGGYGTMMRKYGLSVDNVVGSRIIDSNGNTYFDRMSMGEELFWAVRGGGAASFGIVMGYKIRLVPVPEKVTVFSVGKTVGEGAV DLIMKWQNFSHSTDRNLFVKLTLTLVNGTKPGEKTVLATFIGMNLGGLDKTLNVMNRDFPELKLKKTDCTEMRWIDSVLFWAGFPIGTPTSVLLNPRVTK KLFMKRKSDYVKRPVWRTGLGLILKKLVEVGKVEMNWIPYGGRMGEIPSSRTPFPHRGGNLFNIEYIIDWSEAGDDVEKDHLASASEMYKFMTPYVSSNP REAFLNYRDLDIGSGVNSTYQEGKIYGTKYFKDNFERLVDIKTKFDEINFWRNEQSI |
Full Sequence |
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Protein Sequence Length: 527 Download |
MEKLLIICLL LISVSVATSQ SQTDPETFLR CLVREGSNPQ VFISDVTYIP SNSSFTTVLR 60 RRIPNLRFDK PTTPKPIAII TPTTWSHISP ALACARLLPV QVRIRSGGHD FEGLSYTSTA 120 PFFVIDLLNF KSVDVNLTEG TAWVDTGATI GELYYKIAEK SNVLGFPAGL CTTLGVGGHI 180 SGGGYGTMMR KYGLSVDNVV GSRIIDSNGN TYFDRMSMGE ELFWAVRGGG AASFGIVMGY 240 KIRLVPVPEK VTVFSVGKTV GEGAVDLIMK WQNFSHSTDR NLFVKLTLTL VNGTKPGEKT 300 VLATFIGMNL GGLDKTLNVM NRDFPELKLK KTDCTEMRWI DSVLFWAGFP IGTPTSVLLN 360 PRVTKKLFMK RKSDYVKRPV WRTGLGLILK KLVEVGKVEM NWIPYGGRMG EIPSSRTPFP 420 HRGGNLFNIE YIIDWSEAGD DVEKDHLASA SEMYKFMTPY VSSNPREAFL NYRDLDIGSG 480 VNSTYQEGKI YGTKYFKDNF ERLVDIKTKF DEINFWRNEQ SIPVRT* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-9 | 88 | 329 | 261 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-14 | 86 | 209 | 125 | + 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 | 468 | 523 | 56 | + 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 | NP_174359.1 | 0 | 15 | 525 | 16 | 526 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | NP_174360.1 | 0 | 1 | 525 | 1 | 525 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | XP_002317086.1 | 0 | 4 | 526 | 5 | 527 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523152.1 | 0 | 26 | 523 | 10 | 506 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523155.1 | 0 | 9 | 525 | 11 | 524 | 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 | 26 | 523 | 5 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 28 | 523 | 13 | 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 | 523 | 13 | 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 | 523 | 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 | 26 | 523 | 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 |