| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra014886 |
| Family | AA7 |
| Protein Properties | Length: 527 Molecular Weight: 58593.3 Isoelectric Point: 9.6341 |
| Chromosome | Chromosome/Scaffold: 07 Start: 5588380 End: 5589960 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 66 | 522 | 0 |
| LRFDKPTTPKPLAIVAAATWTHIQAALGCARELSLQVRIRSGGHDFEGLSYTSTVPFFVLDMFSFRTVDVNLTDGTAWVDAGVTTGELYYRIAEKSNVLG FPAGLCTTLGVGGHFSGGGYGTIMRKYGLSVDNVVGSGIVDSNGNIFTDRVSMGEDRFWAIRGGGAASFGVVLGYKIRLVPVPEKVTVFNVGRTVAEGAV DLIMKWQSFAHSTDRNLFVRLTLTLVNGTKPGEKMVLASFIGMYLGGSDKTFNVMNRDFPELKLKRTDCTEMRWIESVVFWAGFPTGTPISVLLNRTVTN KAFHKRKSDYVKRPISRIGLGLILKKLVEVENVRMFFNPYGGRMGEIPSSRTPFPHRAGNLYKIEYLVSWSEAGEDVEKNQLARAREMYEFMSPYVSKNP REAFFNYRDLDIGSSVNSTYEEGKVYGVKYFKDNFERLVDIKTLIDAENFWKNEQGI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 527 Download |
| MEKLLVITLL LILNSVATSQ PVTDPVAFLR CLERQPTDPA SPNSAVAYIP TNSSFTTVLR 60 SRIPNLRFDK PTTPKPLAIV AAATWTHIQA ALGCARELSL QVRIRSGGHD FEGLSYTSTV 120 PFFVLDMFSF RTVDVNLTDG TAWVDAGVTT GELYYRIAEK SNVLGFPAGL CTTLGVGGHF 180 SGGGYGTIMR KYGLSVDNVV GSGIVDSNGN IFTDRVSMGE DRFWAIRGGG AASFGVVLGY 240 KIRLVPVPEK VTVFNVGRTV AEGAVDLIMK WQSFAHSTDR NLFVRLTLTL VNGTKPGEKM 300 VLASFIGMYL GGSDKTFNVM NRDFPELKLK RTDCTEMRWI ESVVFWAGFP TGTPISVLLN 360 RTVTNKAFHK RKSDYVKRPI SRIGLGLILK KLVEVENVRM FFNPYGGRMG EIPSSRTPFP 420 HRAGNLYKIE YLVSWSEAGE DVEKNQLARA REMYEFMSPY VSKNPREAFF NYRDLDIGSS 480 VNSTYEEGKV YGVKYFKDNF ERLVDIKTLI DAENFWKNEQ GIPVRR* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 8.0e-13 | 468 | 523 | 56 | + 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-13 | 76 | 278 | 212 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 7.0e-20 | 76 | 213 | 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 | NP_174359.1 | 0 | 15 | 526 | 16 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_174360.1 | 0 | 1 | 526 | 1 | 526 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | XP_002267223.1 | 0 | 28 | 523 | 38 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002317086.1 | 0 | 11 | 525 | 10 | 526 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523155.1 | 0 | 11 | 525 | 11 | 524 | Reticuline oxidase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 28 | 523 | 7 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 28 | 523 | 13 | 494 | 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 | 28 | 523 | 13 | 494 | 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 | 28 | 523 | 11 | 494 | 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 | 28 | 523 | 11 | 494 | 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 |
