Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10010643 |
Family | AA7 |
Protein Properties | Length: 544 Molecular Weight: 60309.5 Isoelectric Point: 5.2233 |
Chromosome | Chromosome/Scaffold: 296 Start: 292217 End: 295890 |
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 | 71 | 530 | 0 |
LRFDSPSTQKPLAIVLPSTVEELFGTVSCCRRHNVAVKVRCGGHSYEGTSFSPGAAGNSDDFVIVDLMRMNGVSVDLESETAWVEGGATLGETYWAIAEA SHDALAFSAGSCPTVGVGGHIAGGGYGLLSRRYGVAADNVVDALLVSANGVLLDRKAMGEEVFWAIRGGGGGTYGIIYAWKINLLKIPPLLTAFTVSRQP SAKSNLSNLLTKWQSVAPNLNPDFYLSCFVGSSLPQAPKPNQISATFKGLYLGPTQAALSTLNSVFPELEIVAADCYEMSWIESVHFFSGLDPVRSSVLD LKDRYFEDKHCFKAKSDYVRDEIPVKGIEEIVQILEREPKGYVILDPYGGKMSEIKSDAIAFPHRKGNLYTIQYLVEWREEEEDIESSAQYVEWIREFYE AMTPFVSKSPRAAYVNYMDFDLGEDARVWGEKYFLNNFDRLVMAKTLIDPNNVFYNRQSI |
Full Sequence |
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Protein Sequence Length: 544 Download |
MAAAAKYSSS LLLLFIFFLF HFPHTTTTSL ISKPTTTLTS CFHQNQIQNF TTLTSNPTTF 60 YTLLRYSIQN LRFDSPSTQK PLAIVLPSTV EELFGTVSCC RRHNVAVKVR CGGHSYEGTS 120 FSPGAAGNSD DFVIVDLMRM NGVSVDLESE TAWVEGGATL GETYWAIAEA SHDALAFSAG 180 SCPTVGVGGH IAGGGYGLLS RRYGVAADNV VDALLVSANG VLLDRKAMGE EVFWAIRGGG 240 GGTYGIIYAW KINLLKIPPL LTAFTVSRQP SAKSNLSNLL TKWQSVAPNL NPDFYLSCFV 300 GSSLPQAPKP NQISATFKGL YLGPTQAALS TLNSVFPELE IVAADCYEMS WIESVHFFSG 360 LDPVRSSVLD LKDRYFEDKH CFKAKSDYVR DEIPVKGIEE IVQILEREPK GYVILDPYGG 420 KMSEIKSDAI AFPHRKGNLY TIQYLVEWRE EEEDIESSAQ YVEWIREFYE AMTPFVSKSP 480 RAAYVNYMDF DLGEDARVWG EKYFLNNFDR LVMAKTLIDP NNVFYNRQSI PTLSSLMELR 540 DDH* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-14 | 78 | 162 | 86 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 4.0e-18 | 483 | 531 | 49 | + 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. | ||
pfam01565 | FAD_binding_4 | 4.0e-19 | 81 | 185 | 106 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI16966.1 | 0 | 3 | 533 | 276 | 767 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 3.9937e-43 | 384 | 511 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 6 | 533 | 3 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 31 | 540 | 10 | 534 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 38 | 533 | 31 | 535 | d-lactate dehydrogenase, 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 | 3fw9_A | 0 | 38 | 534 | 2 | 495 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 38 | 536 | 8 | 503 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 38 | 536 | 8 | 503 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 38 | 536 | 27 | 522 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 38 | 536 | 27 | 522 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |