y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 492803 |
Family | AA7 |
Protein Properties | Length: 575 Molecular Weight: 63817.2 Isoelectric Point: 10.1314 |
Chromosome | Chromosome/Scaffold: 7 Start: 9592092 End: 9594413 |
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 | 80 | 537 | 0 |
NARFNTSSTPKPTIIITPRSESHVSAAVTCSKTLNFLLKIRSGGHDYDGLSYISDKPFFILDLSNIRDVSVDIASNSAWISAGATLGEVYYRIWEKSKVH GFPAGVCPTVGVGGHLSGGGYGNMLRKFGLSVDYVEDAKIVDVNGRVLDRKAMGEDLFWAITGGGGGSYGVVLGYKVKLVPVPSIVTVFRVEQYMDSGAV DMVYKWQSVGPKTDRNLFMRMLIQPVTRKKVKTVRASVVALFLGRADTVVALLRKEFPELGLTKENCSEMTWFQSALWWDNRVNATQEDPKVFLDRNLDT ASFGKRKSDYVATAIPRKGIESLFKKMIELGKIGLVFNPYGGKMAEVAVNATPFPHRNKLFKIQYSVNWKENSAEIEKGYLNQAKVLYSFMTGFVSKNPR SAYFNYRDVDIGVNDHGVNSYKEGEVYGRKYFGENFDRLVKIKTAVDPGNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 575 Download |
MLTTPPRTFV SVPFFFFLLF FSLPLSSLSQ PSPSSSNSVY NSFLKCFSEK TKSPQSQITD 60 NVFSQSNPSF SSVLRAYIRN ARFNTSSTPK PTIIITPRSE SHVSAAVTCS KTLNFLLKIR 120 SGGHDYDGLS YISDKPFFIL DLSNIRDVSV DIASNSAWIS AGATLGEVYY RIWEKSKVHG 180 FPAGVCPTVG VGGHLSGGGY GNMLRKFGLS VDYVEDAKIV DVNGRVLDRK AMGEDLFWAI 240 TGGGGGSYGV VLGYKVKLVP VPSIVTVFRV EQYMDSGAVD MVYKWQSVGP KTDRNLFMRM 300 LIQPVTRKKV KTVRASVVAL FLGRADTVVA LLRKEFPELG LTKENCSEMT WFQSALWWDN 360 RVNATQEDPK VFLDRNLDTA SFGKRKSDYV ATAIPRKGIE SLFKKMIELG KIGLVFNPYG 420 GKMAEVAVNA TPFPHRNKLF KIQYSVNWKE NSAEIEKGYL NQAKVLYSFM TGFVSKNPRS 480 AYFNYRDVDI GVNDHGVNSY KEGEVYGRKY FGENFDRLVK IKTAVDPGNF FRNEQSIPTL 540 KNAKGTLLPE PGKAKRWSRA GGATVVATVV LHVF* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-6 | 103 | 540 | 462 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-13 | 100 | 228 | 130 | + 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 | 2.0e-17 | 481 | 538 | 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. |
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 | 42 | 540 | 6 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 33 | 540 | 3 | 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 | 33 | 540 | 3 | 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 | 3tsj_B | 0 | 62 | 540 | 24 | 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 | 3tsj_A | 0 | 62 | 540 | 24 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |