| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra005392 |
| Family | AA7 |
| Protein Properties | Length: 533 Molecular Weight: 59661.2 Isoelectric Point: 6.8011 |
| Chromosome | Chromosome/Scaffold: 05 Start: 5186824 End: 5189379 |
| 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 | 71 | 305 | 0 |
| NLRYLTPSNPKPVFIFEPMYETHVQAAVVCAKKLQLHMRVRSGGHDYEGLSFVSENETPFVIVDLSKLRQIDVDVDSNSAWAHAGATVGEVYYRIQEKSQ THGFPAGLCSSLGIGGHLVGGAYGSMMRKFGLGADNVLDARIIDANGKILDRAAMGEDVFWALRGGGGGSFGVILAWKIKLVPVPATVTVFTVTKTLEQD GTKVLYKWQQVADKLDEDLFIRVIIQTASKTTKPG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 533 Download |
| MAFAVSKRNA MAFAVTLLLV SIPMSSSTLQ QDFLQCLVEN SDISFPITAA FYSPDQNATL 60 FKEELESTAQ NLRYLTPSNP KPVFIFEPMY ETHVQAAVVC AKKLQLHMRV RSGGHDYEGL 120 SFVSENETPF VIVDLSKLRQ IDVDVDSNSA WAHAGATVGE VYYRIQEKSQ THGFPAGLCS 180 SLGIGGHLVG GAYGSMMRKF GLGADNVLDA RIIDANGKIL DRAAMGEDVF WALRGGGGGS 240 FGVILAWKIK LVPVPATVTV FTVTKTLEQD GTKVLYKWQQ VADKLDEDLF IRVIIQTASK 300 TTKPGNRTIS TSYQGQFLGD SNRLMQVMQK SFPELGLTKK DCTEMSWIKS VMYIAGFPSS 360 AAPEALLDGK SLFKSYFKAK SDFVEEPIPV EGLEGLWKKL LEEDSPLTIW NPYGGVMSRI 420 AESEIPFPHR KGTLFKIQWL SSWSDGKASD ERHMKWMREM YSYMEKYVSK NPRRAYVNYR 480 DLDLGVNEEE SDAREWGTKY FKGNFERLVK IKGEFDPENF FRHEQSIPTK IG* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01679 | bact_FAD_ox | 0.0004 | 82 | 244 | 165 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
| COG0277 | GlcD | 6.0e-20 | 94 | 251 | 167 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam08031 | BBE | 6.0e-21 | 475 | 528 | 54 | + 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. | ||
| pfam01565 | FAD_binding_4 | 5.0e-26 | 82 | 221 | 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. | ||
| 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_174363.1 | 0 | 27 | 531 | 29 | 533 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_181025.1 | 0 | 1 | 532 | 1 | 532 | MEE23 (MATERNAL EFFECT EMBRYO ARREST 23); FAD binding / catalytic/ electron carrier/ oxidoreductase [Arabidopsis thaliana] |
| RefSeq | XP_002268361.1 | 0 | 9 | 528 | 5 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002523162.1 | 0 | 33 | 528 | 33 | 529 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 0 | 33 | 528 | 33 | 529 | 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 | 30 | 528 | 4 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 23 | 528 | 3 | 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 | 23 | 528 | 3 | 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 | 30 | 531 | 8 | 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_A | 0 | 30 | 531 | 8 | 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 |
