| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 473604 |
| Family | AA7 |
| Protein Properties | Length: 368 Molecular Weight: 40617.5 Isoelectric Point: 8.9567 |
| Chromosome | Chromosome/Scaffold: 1 Start: 16376585 End: 16377779 |
| 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 | 69 | 263 | 0 |
| RNLRYFNGITRKPVAIVAAAHFTHIQATINCAKKLGLQLRIRSGGHDYDGMSYLSTVDFVVLDMFNLRSIEIDPKLDTACVQSGATLGEIYYNVANKSNN LRGFPAGICPGLGARGHFSGGGYGNMMRKYGLSIDNNIDAKTVDANARVLDRSSMGEDLFWAIRGGGAASFCVVLAWKIKLVPVPEKVTVSIVDL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 368 Download |
| MKSSTTQTII VTFFLLIIPT SFAAPPKLED SFTQCLTTFK PSDPKFPIQN FTYTQENPNF 60 LIILNNYVRN LRYFNGITRK PVAIVAAAHF THIQATINCA KKLGLQLRIR SGGHDYDGMS 120 YLSTVDFVVL DMFNLRSIEI DPKLDTACVQ SGATLGEIYY NVANKSNNLR GFPAGICPGL 180 GARGHFSGGG YGNMMRKYGL SIDNNIDAKT VDANARVLDR SSMGEDLFWA IRGGGAASFC 240 VVLAWKIKLV PVPEKVTVSI VDLGRSPVLP IFNVETVGNR GGIQYSSNWF VPGEEAASDC 300 LSQTERVFKA MSPYVSKNPR EAFLNYRDVD IGKNLNSTYE EGKSWFRLRL ELIPTTFSGT 360 SRAFQCT* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 4.0e-13 | 64 | 263 | 212 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 3.0e-21 | 81 | 221 | 143 | + 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 |
| GenBank | AAF79255.1 | 0 | 1 | 283 | 1 | 267 | AC023279_4 F12K21.9 [Arabidopsis thaliana] |
| GenBank | AAF79255.1 | 3e-31 | 278 | 345 | 423 | 490 | AC023279_4 F12K21.9 [Arabidopsis thaliana] |
| RefSeq | NP_174358.1 | 0 | 1 | 283 | 1 | 270 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_564449.1 | 0 | 1 | 283 | 1 | 267 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_564449.1 | 9e-32 | 278 | 345 | 423 | 490 | 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 | 30 | 258 | 5 | 230 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3vte_A | 0.000004 | 279 | 345 | 408 | 479 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 23 | 264 | 1 | 239 | 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_B | 0.0000000004 | 283 | 345 | 398 | 462 | 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 | 264 | 1 | 239 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
