y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.F04104.1 |
Family | AA7 |
Protein Properties | Length: 494 Molecular Weight: 53721.1 Isoelectric Point: 5.8457 |
Chromosome | Chromosome/Scaffold: 6 Start: 49306876 End: 49308477 |
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 | 243 | 0 |
LRFSGPAVPKPVAIIFPGSVEQLKSSIVCCREGAWEIRVRSGGHSYEGTSWVATDGAPFVVVDMMNLNGVRVDLDTMTAWVEGGATLGETYYAIAEASDV HGFSAGSCPTVGVGGHISGGGFGLLSRKYGLAADNVVDALLVDSRGRLLDRKAMGEDVFWAIRGGGGGLWGIIYAWKIKLLNVPRKVTGFIMR |
Full Sequence |
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Protein Sequence Length: 494 Download |
MSLSAPALCS SADSIASCLT QHNVNNFTTF PATENESARY YELLNSSIHN LRFSGPAVPK 60 PVAIIFPGSV EQLKSSIVCC REGAWEIRVR SGGHSYEGTS WVATDGAPFV VVDMMNLNGV 120 RVDLDTMTAW VEGGATLGET YYAIAEASDV HGFSAGSCPT VGVGGHISGG GFGLLSRKYG 180 LAADNVVDAL LVDSRGRLLD RKAMGEDVFW AIRGGGGGLW GIIYAWKIKL LNVPRKVTGF 240 IMRTIGISAT FKGFFLGPRT EAVSLLNRKF PELGIEEEDC KEMSWIESIL FFSGLGDGST 300 ILDLKNRFID YKYYKAKSDY VRSPISLSGI LEALDILEAE PKGYVILDPY GGIMHKISGE 360 SIAFPHREGN LFTIQYLVEW HENDNEVRDG YLNWIRGFHD SMAAHVSSGP RAAYVNYMDL 420 DLGVTGLIDP SAGKDDAVEI ARAWGEKYFL GNYERLVRAK TKIDPLNVFR NQQGIPPMPP 480 GGGARAGRLD AAK* 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-15 | 61 | 235 | 182 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 2.0e-16 | 413 | 475 | 63 | + 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 | 5.0e-23 | 61 | 200 | 141 | + 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 | 1 | 479 | 293 | 768 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 0 | 316 | 456 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 1 | 482 | 17 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 1 | 477 | 3 | 525 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 3 | 486 | 19 | 544 | 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 | 3d2j_A | 0 | 9 | 478 | 20 | 519 | A Chain A, Diferric Chicken Serum Transferrin At 2.8 A Resolution. |
PDB | 3d2h_A | 0 | 9 | 478 | 20 | 519 | A Chain A, Diferric Chicken Serum Transferrin At 2.8 A Resolution. |
PDB | 3d2d_A | 0 | 9 | 478 | 20 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 15 | 478 | 2 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 9 | 478 | 2 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 519 | 6 | 475 | 0 |
FC883009 | 247 | 5 | 246 | 0 |
DY275245 | 243 | 5 | 242 | 0 |
DY806824 | 256 | 1 | 250 | 0 |
DY275245 | 85 | 247 | 324 | 0.91 |
Sequence Alignments (This image is cropped. Click for full image.) |
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