Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.D01625.1 |
Family | AA7 |
Protein Properties | Length: 529 Molecular Weight: 58766.2 Isoelectric Point: 7.8786 |
Chromosome | Chromosome/Scaffold: 4 Start: 30104988 End: 30106574 |
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 | 68 | 519 | 0 |
NTSSPSPQLIVTPVNPSQIQAAIVCSQKLGVHVRVRSGGHDYEGLSYVSQMPFIIIDLRNMRLVEVDVEKESAWVETGATVGELYYAISQKSKVLGFPAG SCPTVGVGGQVSGGGVGTIFRKYGLAADNVIDAKIVDVNGKVLDRKAMGEDLFWAIRGGGGASFGVIFAWKFVLVPVPPTVTVFEVGKTIEEDATMLLYK WQNVAHKLHEDLFLHAVTGVVTPSSSLANKTISISFGGLYLGKIEKLLPSIQESFPELGLTRESCTEMSWIQSVLYFAGFSQDGSPEVLLNRTQSSRSFF KAKSDFVMEPISQTALQGLWNKLIEDETSYLILTPYGGVMSQISDSATPFPHRGGNMYQIMYMVTWDSEEENNQKINWMRELYDYMAPYVSRFPRAAYMN YRDLDLGRNYVINTTYAQASVWGLKYFKSNFKRLVKVKTASDPANFFWNEQS |
Full Sequence |
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Protein Sequence Length: 529 Download |
MAANLPLISI IFLSFCYVAS SFDQVSFLQC FSLHSFQSNS TSKTITTRKD PTYISLLQSS 60 IQNLRFLNTS SPSPQLIVTP VNPSQIQAAI VCSQKLGVHV RVRSGGHDYE GLSYVSQMPF 120 IIIDLRNMRL VEVDVEKESA WVETGATVGE LYYAISQKSK VLGFPAGSCP TVGVGGQVSG 180 GGVGTIFRKY GLAADNVIDA KIVDVNGKVL DRKAMGEDLF WAIRGGGGAS FGVIFAWKFV 240 LVPVPPTVTV FEVGKTIEED ATMLLYKWQN VAHKLHEDLF LHAVTGVVTP SSSLANKTIS 300 ISFGGLYLGK IEKLLPSIQE SFPELGLTRE SCTEMSWIQS VLYFAGFSQD GSPEVLLNRT 360 QSSRSFFKAK SDFVMEPISQ TALQGLWNKL IEDETSYLIL TPYGGVMSQI SDSATPFPHR 420 GGNMYQIMYM VTWDSEEENN QKINWMRELY DYMAPYVSRF PRAAYMNYRD LDLGRNYVIN 480 TTYAQASVWG LKYFKSNFKR LVKVKTASDP ANFFWNEQSF PVSSPGRR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 0.001 | 74 | 234 | 164 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
pfam08031 | BBE | 1.0e-15 | 464 | 521 | 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 | 7.0e-20 | 74 | 521 | 461 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-23 | 74 | 211 | 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAN81654.1 | 0 | 3 | 521 | 7 | 525 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268361.1 | 0 | 3 | 521 | 7 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299029.1 | 0 | 20 | 522 | 1 | 502 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317088.1 | 0 | 4 | 522 | 7 | 526 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523160.1 | 0 | 4 | 524 | 8 | 528 | 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 | 525 | 6 | 515 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 26 | 521 | 12 | 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 | 26 | 521 | 12 | 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 | 43 | 521 | 22 | 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 | 43 | 521 | 22 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |