| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT4G20860.1 |
| Family | AA7 |
| Protein Properties | Length: 531 Molecular Weight: 60409.5 Isoelectric Point: 9.452 |
| Chromosome | Chromosome/Scaffold: 4 Start: 11172622 End: 11174467 |
| Description | reticuline oxidase-like protein precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 75 | 294 | 0 |
| NFTSLKPILIVKPKSESEIKQSILCSRKLGVQVRTMSGGHDYEGLSYLSLSPFIIVDLVNLRSISINLTDETAWIQSGATLGEVYYKIAKTSKIHAFAAG ICPSVGVGGHISGGGFGTIMRKYGLASDNVVDARLMDVNGKTLDRKTMGEDLFWALRGGGAASFGVVLSWKVKLARVPEKVTCFISQHPMGPSMNKLVHR WQSIGSELDEDLFIRVIIDN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 531 Download |
| MRELFMYLFL LFLVLCVKSV YSTPTREQFQ NCLSTKQFNS TLKNPINLTT HTLDSRVHTD 60 FSESSSPNSS FLNLNFTSLK PILIVKPKSE SEIKQSILCS RKLGVQVRTM SGGHDYEGLS 120 YLSLSPFIIV DLVNLRSISI NLTDETAWIQ SGATLGEVYY KIAKTSKIHA FAAGICPSVG 180 VGGHISGGGF GTIMRKYGLA SDNVVDARLM DVNGKTLDRK TMGEDLFWAL RGGGAASFGV 240 VLSWKVKLAR VPEKVTCFIS QHPMGPSMNK LVHRWQSIGS ELDEDLFIRV IIDNSLEGNQ 300 RKVKSTFQTL FLGGIDRLIP LMNQKFPELG LRSQDCSEMS WIESIMFFNW RSGQPLEILL 360 NRDLRFEDQY FKAKSDYVQK PVPENVFEEV TKRFLEQDTP LMIFEPLGGK ISKISETESP 420 YPHRRGNLYN IQYMVKWKVN EVEEMNKHVR WMRSLHDYMT PYVSKSPRGA YLNYRDLDLG 480 STKGINTSFE DARKWGETYF KGNFKRLGLV KGKIDPTNFF RNEQSIPPLF * 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 1.0e-11 | 81 | 529 | 475 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-17 | 81 | 218 | 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. | ||
| pfam08031 | BBE | 9.0e-18 | 470 | 527 | 58 | + 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:0003824 | catalytic activity |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0009055 | electron carrier activity |
| GO:0010583 | response to cyclopentenone |
| GO:0012505 | endomembrane system |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAK56258.1 | 0 | 1 | 530 | 1 | 530 | AF367269_1 AT4g20860/T13K14_20 [Arabidopsis thaliana] |
| GenBank | AAN60251.1 | 0 | 1 | 453 | 1 | 451 | unknown [Arabidopsis thaliana] |
| RefSeq | NP_193818.1 | 0 | 1 | 530 | 1 | 530 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_199249.1 | 0 | 1 | 529 | 1 | 530 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | XP_002523167.1 | 0 | 1 | 527 | 1 | 522 | 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 | 26 | 529 | 4 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_B | 0 | 78 | 530 | 50 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_A | 0 | 78 | 530 | 50 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsh_A | 0 | 78 | 530 | 50 | 497 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 4dns_B | 0 | 68 | 530 | 39 | 497 | 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 |
