y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.D00089.1 |
Family | AA7 |
Protein Properties | Length: 517 Molecular Weight: 58508.2 Isoelectric Point: 8.1793 |
Chromosome | Chromosome/Scaffold: 4 Start: 1432778 End: 1434641 |
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 | 51 | 506 | 0 |
SSRSSLKPLLIVTPFHESEIQAAILCTKKHGLQIRVRSGGHDYEGLSYRCKTPFILVDLVNLRSVDINLEEEVAWVQSGATLGELYYSIAMESKVHGFPA GICPSVGIGGHLSGGGFGTMLRKHGLAADNVIDAYLIDVSGRILNRELMGEDLFWAIRGGGGASFGIILSWKIKLVRVPPTVTVFTVSRSLEQGAIELVH RWQYIAHELSEDLFIRVIIQDVDDPNNGAARTVQAAFNSLFLGKLDCLMPLMNQSFPELGLKVDNCTEMTWIESVLYFAGYKKDDPLEVLLDRNTLYKSY FKAKSDFAQEPIPEVGLRVIWERFLEEEIVFMIMDPYGGKMNEIPESELPFPHRRGNLYNVQYLVKWVQNGVKASKKHLHWMRMLYNYMTPYVSASPRAA YLNYRDLDLGINGKGEESYSGASVWGVKYFKDNFKRLAIVKGRVDPENFLRSEQSI |
Full Sequence |
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Protein Sequence Length: 517 Download |
MGWFKFANRW GQKAQTIIDY TKTFEIIYSS NSSSYPHLLQ SSEQNPRWVN SSRSSLKPLL 60 IVTPFHESEI QAAILCTKKH GLQIRVRSGG HDYEGLSYRC KTPFILVDLV NLRSVDINLE 120 EEVAWVQSGA TLGELYYSIA MESKVHGFPA GICPSVGIGG HLSGGGFGTM LRKHGLAADN 180 VIDAYLIDVS GRILNRELMG EDLFWAIRGG GGASFGIILS WKIKLVRVPP TVTVFTVSRS 240 LEQGAIELVH RWQYIAHELS EDLFIRVIIQ DVDDPNNGAA RTVQAAFNSL FLGKLDCLMP 300 LMNQSFPELG LKVDNCTEMT WIESVLYFAG YKKDDPLEVL LDRNTLYKSY FKAKSDFAQE 360 PIPEVGLRVI WERFLEEEIV FMIMDPYGGK MNEIPESELP FPHRRGNLYN VQYLVKWVQN 420 GVKASKKHLH WMRMLYNYMT PYVSASPRAA YLNYRDLDLG INGKGEESYS GASVWGVKYF 480 KDNFKRLAIV KGRVDPENFL RSEQSIPPYP ALKKGR* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 3.0e-12 | 58 | 225 | 177 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 4.0e-15 | 450 | 507 | 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. | ||
pfam01565 | FAD_binding_4 | 2.0e-18 | 58 | 195 | 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 |
GenBank | ABC41950.1 | 0 | 25 | 507 | 45 | 521 | FAD-linked oxidoreductase 1 [Glycine max] |
GenBank | ABC41951.1 | 0 | 25 | 507 | 45 | 522 | FAD-linked oxidoreductase 2 [Glycine max] |
RefSeq | XP_002267029.1 | 0 | 20 | 516 | 283 | 777 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002330615.1 | 0 | 20 | 507 | 46 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523167.1 | 0 | 20 | 509 | 37 | 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 | 25 | 510 | 23 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 27 | 508 | 26 | 495 | 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 | 27 | 508 | 26 | 495 | 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 | 25 | 508 | 22 | 495 | 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 | 25 | 508 | 22 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 489 | 26 | 507 | 0 |
CV529433 | 316 | 43 | 357 | 0 |
FE675676 | 285 | 77 | 361 | 0 |
EX137437 | 304 | 62 | 364 | 0 |
EG029578 | 294 | 169 | 460 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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