y
Basic Information | |
---|---|
Species | Mimulus guttatus |
Cazyme ID | mgv1a020959m |
Family | AA7 |
Protein Properties | Length: 411 Molecular Weight: 45419.6 Isoelectric Point: 4.635 |
Chromosome | Chromosome/Scaffold: 102 Start: 327486 End: 328718 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA7 | 1 | 397 | 0 |
VSVDLESNTAWVEGGATLGQTYYSISQASGGLGFSAGSCPTVGIGGHISGGGFGLLSRKYGVAADNVVDALLIDADGRLLDRVAMGEEVFWAIRGGGGGV WGVVYAWKIELLEVPQIVTGFVVSRPGSKRAVVDLVEKWQEVAPNLEEGFYLSCFVGAHLPEMESLGISATFKGFYLGPKVEAVSIMNEVFQELGVVEGD CKEMSWIESIVYFSGLRNGSSVSSLKDRYLEEKNYFKAKSDYVRDLIPRSGIAYAIEILEKEPKGYVILDPYGGIMERISSESIAFPHRKGNLFTIQYLV EWKEEDNGRREDYIDWIRGFYDAMAPYVSFKPRAAYVNYVDFDLGVVDFLNRSGYGGDDVEVARVWGEKYFLKNYDRLVRAKTVIDPFNVFRNQQGI |
Full Sequence |
---|
Protein Sequence Length: 411 Download |
VSVDLESNTA WVEGGATLGQ TYYSISQASG GLGFSAGSCP TVGIGGHISG GGFGLLSRKY 60 GVAADNVVDA LLIDADGRLL DRVAMGEEVF WAIRGGGGGV WGVVYAWKIE LLEVPQIVTG 120 FVVSRPGSKR AVVDLVEKWQ EVAPNLEEGF YLSCFVGAHL PEMESLGISA TFKGFYLGPK 180 VEAVSIMNEV FQELGVVEGD CKEMSWIESI VYFSGLRNGS SVSSLKDRYL EEKNYFKAKS 240 DYVRDLIPRS GIAYAIEILE KEPKGYVILD PYGGIMERIS SESIAFPHRK GNLFTIQYLV 300 EWKEEDNGRR EDYIDWIRGF YDAMAPYVSF KPRAAYVNYV DFDLGVVDFL NRSGYGGDDV 360 EVARVWGEKY FLKNYDRLVR AKTVIDPFNV FRNQQGIPPL DVVKYGKAEI * 420 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 0.006 | 1 | 400 | 408 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 6.0e-9 | 1 | 81 | 81 | + 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. | ||
pfam08031 | BBE | 3.0e-14 | 335 | 398 | 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. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0016491 | oxidoreductase activity |
GO:0050660 | flavin adenine dinucleotide binding |
GO:0055114 | oxidation-reduction process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAC65012.1 | 0 | 1 | 400 | 133 | 537 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
GenBank | EAZ05661.1 | 0 | 1 | 400 | 133 | 537 | hypothetical protein OsI_27888 [Oryza sativa Indica Group] |
RefSeq | XP_002264336.1 | 0 | 1 | 400 | 136 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 1 | 399 | 124 | 525 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 1 | 410 | 136 | 546 | d-lactate dehydrogenase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3fw9_A | 0 | 1 | 400 | 103 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 3fw7_A | 0 | 1 | 400 | 106 | 497 | A Chain A, Structure Of Berberine Bridge Enzyme, H104a Variant |
PDB | 4ec3_A | 0 | 1 | 405 | 109 | 505 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 1 | 405 | 109 | 505 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 1 | 405 | 128 | 524 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
EL451713 | 301 | 110 | 409 | 0 |
GO028240 | 273 | 128 | 400 | 0 |
HO777438 | 413 | 1 | 405 | 0 |
ES434378 | 278 | 32 | 309 | 0 |
FG166662 | 238 | 177 | 400 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|