| Basic Information | |
|---|---|
| Species | Populus trichocarpa |
| Cazyme ID | Potri.011G162900.1 |
| Family | AA7 |
| Protein Properties | Length: 534 Molecular Weight: 59596 Isoelectric Point: 6.9118 |
| Chromosome | Chromosome/Scaffold: 11 Start: 18042298 End: 18044178 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 74 | 290 | 0 |
| KLTPVVIVTPTILSHIQATIHCSQKHNLQIRIRSGGHDYEGLSYMSVLPFVILDLINLRKITVDLSTKTAWVQAGATLGELYYSIAEKSRTLAFPAGACH TVGVGGQFSGGGYGGLLRKYGLAADNVIDAELIDANGRVLDRESMGEDLFWAIRGGGGNSFGVVTAWKVNLVEVPPTVTVFAVPKVLKENATKLIHRWQY VANKLPEDIVIAAYVNR | |||
| Full Sequence |
|---|
| Protein Sequence Length: 534 Download |
| MTSLSSSMLP FLLILLFPFS WGTSAHTHED FLQCLSLYSE DSAATSKVIY TPNNTSYATV 60 LQFSIRNLRF NSSKLTPVVI VTPTILSHIQ ATIHCSQKHN LQIRIRSGGH DYEGLSYMSV 120 LPFVILDLIN LRKITVDLST KTAWVQAGAT LGELYYSIAE KSRTLAFPAG ACHTVGVGGQ 180 FSGGGYGGLL RKYGLAADNV IDAELIDANG RVLDRESMGE DLFWAIRGGG GNSFGVVTAW 240 KVNLVEVPPT VTVFAVPKVL KENATKLIHR WQYVANKLPE DIVIAAYVNR INSSQGGNPT 300 IQATFTSLFL GGVDRLLPLM QESFPELGLV KDDCIELSWI EFALFLAGFP SNASLDVLLD 360 RTPQSITSFK AKSDYVKQPL PETALEGMWE TFFEKDIESP SLFMVPYGGK MEEISESSIP 420 FPHRAGNLYK IHYYVAWTEE GKEASERHIS WIRRLYSYMT PYVSKNPREA YVNYRDLDLG 480 INNLAGNTSY KQASIWGRKY FKNNFDKLVR IKTEVDPANF FRNEQSIPPF SSW* 540 |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam08031 | BBE | 3.0e-18 | 470 | 528 | 59 | + 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 | 1.0e-22 | 77 | 530 | 471 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
| pfam01565 | FAD_binding_4 | 8.0e-25 | 77 | 214 | 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_002299045.1 | 0 | 1 | 533 | 1 | 533 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002330609.1 | 0 | 1 | 533 | 1 | 534 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002333020.1 | 0 | 1 | 533 | 1 | 533 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002333338.1 | 0 | 1 | 533 | 1 | 533 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002333339.1 | 0 | 1 | 533 | 1 | 533 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 25 | 530 | 1 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 24 | 530 | 6 | 496 | 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 | 24 | 530 | 6 | 496 | 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 | 29 | 530 | 9 | 496 | 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 | 29 | 530 | 9 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |
