| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT1G26380.1 |
| Family | AA7 |
| Protein Properties | Length: 536 Molecular Weight: 59817.6 Isoelectric Point: 7.9636 |
| Chromosome | Chromosome/Scaffold: 1 Start: 9126737 End: 9128528 |
| Description | reticuline oxidase-like protein precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 66 | 297 | 0 |
| NTRFSNPNNKNLLAIVVAKDVSHVQATVVCAKSNGIQIRIRSGGHDNEGLSYVSSVPFVILDMHKLRDITVDVSSKKAWVQAGATLGELYVKIDEASQTL AFPAGICATVGAGGHISGGGYGNLMRKFGTTVDHVIDAELVDVNGKLLNRSTMGEDLFWAIRGGGGASFGVILSWKINLVEVPKIFTVFQVNKTLEQGGT DVVYKWQLVANKFPDNLFLRAMPQVVNGTKHG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 536 Download |
| MKEALFGLYL VLLVSGLEAA VTKPNSGNFI ECLRYQASPE NPITDAIFTV DNTTTFLSSY 60 VSYTKNTRFS NPNNKNLLAI VVAKDVSHVQ ATVVCAKSNG IQIRIRSGGH DNEGLSYVSS 120 VPFVILDMHK LRDITVDVSS KKAWVQAGAT LGELYVKIDE ASQTLAFPAG ICATVGAGGH 180 ISGGGYGNLM RKFGTTVDHV IDAELVDVNG KLLNRSTMGE DLFWAIRGGG GASFGVILSW 240 KINLVEVPKI FTVFQVNKTL EQGGTDVVYK WQLVANKFPD NLFLRAMPQV VNGTKHGERT 300 IAIVFWAQFL GRTDELMEIM NQSFPELGLR REDCQEMSWL NTTLFWAMLP AGTPKTVLLG 360 RPTDPVFFKS KSDYVKKPIP KEGLEKIWKT MLKFNNIVWL HFNPYGGMMD RIPSNATAFP 420 HRKGNLFKVQ YYTTWLDPNA TESNLSIMKE LYEVAEPYVS SNPREAFFNY RDIDIGSNPS 480 GETDVDEAKI YGYKYFLGNL KRLMDVKAKS DPENFFKNEQ SIPPLLSRVR RDDEL* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 8.0e-13 | 466 | 523 | 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. | ||
| COG0277 | GlcD | 6.0e-21 | 78 | 525 | 474 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 1.0e-21 | 78 | 216 | 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 | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0009055 | electron carrier activity |
| GO:0012505 | endomembrane system |
| GO:0016491 | oxidoreductase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAK93677.1 | 0 | 18 | 525 | 18 | 527 | unknown protein [Arabidopsis thaliana] |
| RefSeq | NP_173965.1 | 0 | 15 | 525 | 39 | 549 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_173966.1 | 0 | 1 | 525 | 1 | 525 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_564244.1 | 0 | 1 | 535 | 1 | 535 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_564245.1 | 0 | 18 | 525 | 18 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| 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 | 525 | 6 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 28 | 526 | 12 | 497 | 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 | 526 | 12 | 497 | 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 | 528 | 10 | 499 | 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 | 528 | 10 | 499 | 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 |
