| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 880898 |
| Family | AA7 |
| Protein Properties | Length: 456 Molecular Weight: 50582.7 Isoelectric Point: 9.7382 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 119 | 255 | 0 |
| TTLGELYTKINEASQTLAFPAGVCPTVGVGGHISGGGFGNLMRKFGITVDHVIDAQLINCNGKLLDRATMGEDLFWAIRGGGGASFGVILSWKINLVEVP KILTVFKVRKTLEQGGTDVLYKWQLVASKFPEDLFIR | |||
| Full Sequence |
|---|
| Protein Sequence Length: 456 Download |
| MKASLSVLCL VLLVSVLEAA VTTKPNSGIF IGCLRNRTSP ENPITDAIFT ADNTTTFLSS 60 YVSYTRNKRY SSPNYQKLIA IVAAKHVSHV QATVICAKTN GIQLRIRSGG HDYEGLSYTT 120 LGELYTKINE ASQTLAFPAG VCPTVGVGGH ISGGGFGNLM RKFGITVDHV IDAQLINCNG 180 KLLDRATMGE DLFWAIRGGG GASFGVILSW KINLVEVPKI LTVFKVRKTL EQGGTDVLYK 240 WQLVASKFPE DLFIRAWPQI VKGTKLGKRT IAVVFFAQFL GPTDKLMAIM SQSLPELGLR 300 RDDCHEMSWF YTTLFWANYP VGTPKRVLLD RPSSPGEFFK SKSDNIKKPI PKEGLEKIWK 360 TMLKFNFETE NKMTMMKELY EVAGPYVSSN PREALLNFRD VDIGSNPSGV NVDEAKIYGY 420 KYFLGNLKRL MDIKAKCDAE NFFKNEQSIS PARVM* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 5.0e-6 | 80 | 302 | 270 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 8.0e-10 | 80 | 184 | 135 | + 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 | 7.0e-10 | 394 | 449 | 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. | ||
| 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 | AAK93677.1 | 0 | 18 | 455 | 18 | 530 | unknown protein [Arabidopsis thaliana] |
| RefSeq | NP_173964.1 | 0 | 1 | 455 | 1 | 527 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_173966.1 | 0 | 1 | 455 | 1 | 528 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_564244.1 | 0 | 1 | 451 | 1 | 524 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_564245.1 | 0 | 18 | 455 | 18 | 530 | 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 | 3tsj_B | 0 | 30 | 451 | 11 | 495 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
| PDB | 3tsj_A | 0 | 30 | 451 | 11 | 495 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
| PDB | 3tsh_A | 0 | 30 | 451 | 11 | 495 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 3vte_A | 0 | 30 | 451 | 7 | 512 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 30 | 451 | 13 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
