Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_014_00740.1 |
Family | AA7 |
Protein Properties | Length: 502 Molecular Weight: 56133 Isoelectric Point: 5.234 |
Chromosome | Chromosome/Scaffold: 14 Start: 4325128 End: 4326635 |
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 | 29 | 483 | 0 |
LEPVVIVLPESKEQLSATILCCQENSVVFTIRSGGHSFEGLSYSAGTRAFIMIDLMNLNKVLVDLESKTAWVEGGATVGEIYHAIGRSSNHLGFPAGLCP AVGSGGHIGGGGYGLMSRKFGLASDNVLDAILVNADGRLLNRKTMGEEVFWAVRGGGAGNWGAIYSWKIQLIDVPETVTAFRISRRGSKTEAAELLSKWQ LVAPNLEDEFSLMVSVVGESETSILSIFQGLYLGRKTSALVSIAHNYPELELLANECNEMTWVESMAYFPGIAEGFTVDALKERFAMCSQKFYYKWKGDY VRDSVSTEGIEGLLHMLMEEPRGQLELSPLGGMMSRIKSDVFPYPHRNGNLYAIGYLVAWGEEDDAHNGVYMNWIRNVHEYMTPFVSKEPRAAYVNEVDL DLGVMDWENHNISMEEFVKLGRTWGEKYFLKNYDRLVRAKTLIDPYNVFRHRQSI |
Full Sequence |
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Protein Sequence Length: 502 Download |
VNHTIPSTPS FNRFFILSSY NLRITKSSLE PVVIVLPESK EQLSATILCC QENSVVFTIR 60 SGGHSFEGLS YSAGTRAFIM IDLMNLNKVL VDLESKTAWV EGGATVGEIY HAIGRSSNHL 120 GFPAGLCPAV GSGGHIGGGG YGLMSRKFGL ASDNVLDAIL VNADGRLLNR KTMGEEVFWA 180 VRGGGAGNWG AIYSWKIQLI DVPETVTAFR ISRRGSKTEA AELLSKWQLV APNLEDEFSL 240 MVSVVGESET SILSIFQGLY LGRKTSALVS IAHNYPELEL LANECNEMTW VESMAYFPGI 300 AEGFTVDALK ERFAMCSQKF YYKWKGDYVR DSVSTEGIEG LLHMLMEEPR GQLELSPLGG 360 MMSRIKSDVF PYPHRNGNLY AIGYLVAWGE EDDAHNGVYM NWIRNVHEYM TPFVSKEPRA 420 AYVNEVDLDL GVMDWENHNI SMEEFVKLGR TWGEKYFLKN YDRLVRAKTL IDPYNVFRHR 480 QSIPPMFFQD LEDDMNQFIS C* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02805 | PLN02805 | 0.001 | 31 | 237 | 222 | + D-lactate dehydrogenase [cytochrome] | ||
pfam08031 | BBE | 4.0e-15 | 421 | 484 | 64 | + 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 | 2.0e-23 | 31 | 485 | 470 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 6.0e-25 | 31 | 169 | 140 | + 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 |
PDB | 3FW9 | 0 | 2 | 486 | 13 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)- Scoulerine |
GenBank | AAD17487.1 | 0 | 2 | 491 | 34 | 521 | berberine bridge enzyme [Berberis stolonifera] |
GenBank | AAU20769.1 | 0 | 1 | 487 | 37 | 519 | berberine bridge enzyme [Thalictrum flavum subsp. glaucum] |
RefSeq | XP_002264336.1 | 0 | 3 | 487 | 48 | 535 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533924.1 | 0 | 17 | 486 | 62 | 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 | 2 | 486 | 13 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 2 | 486 | 19 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 2 | 486 | 19 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 2 | 486 | 38 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 2 | 486 | 38 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 488 | 7 | 484 | 0 |
EL451713 | 295 | 198 | 486 | 0 |
JG649754 | 188 | 317 | 502 | 0 |
DT740104 | 266 | 11 | 274 | 0 |
EB740763 | 301 | 186 | 486 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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