| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_076_00041.2 |
| Family | AA1 |
| Protein Properties | Length: 444 Molecular Weight: 49219 Isoelectric Point: 8.2448 |
| Chromosome | Chromosome/Scaffold: 76 Start: 276707 End: 281137 |
| Description | Plant L-ascorbate oxidase |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA1 | 1 | 416 | 0 |
| MQRSAGLYGSLIVDVADGEKEPFHYDGELNLLLSDWWHQNVHEQEIGLSSNPMRWIGEPQSILMNGKGQYNCSLAGHLSKKTSLCKLRADAQCAPPILHV LPNKTYRLRLASTTSLASLNLAIGHHKMVLVEADGNYVQPVTLDDIDIYSGESYSVLITTNQNPSMNYWVSLGVRGRHPATPPGLTILNYHPNTARPPSS PLPIHAAWDDYPHSKAIANKILALQGSPKPPTRYDRRIYLLNTQNKINGFTKWSINNVSLALPSTPYLGSIKFGLKGAFDHQSPPENFSSEYDVMKPPSN PNSTVSSGVYKLEFGKTIDVILQNANALNANVSEIHPWHLHGHDFWVLGYGEGKFSEEKHSKNLNLKNPPLRNTVVIFPYGWTAIRFVTDNPGVWAFHCH IEPHLHMGMGVIFAES | |||
| Full Sequence |
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| Protein Sequence Length: 444 Download |
| MQRSAGLYGS LIVDVADGEK EPFHYDGELN LLLSDWWHQN VHEQEIGLSS NPMRWIGEPQ 60 SILMNGKGQY NCSLAGHLSK KTSLCKLRAD AQCAPPILHV LPNKTYRLRL ASTTSLASLN 120 LAIGHHKMVL VEADGNYVQP VTLDDIDIYS GESYSVLITT NQNPSMNYWV SLGVRGRHPA 180 TPPGLTILNY HPNTARPPSS PLPIHAAWDD YPHSKAIANK ILALQGSPKP PTRYDRRIYL 240 LNTQNKINGF TKWSINNVSL ALPSTPYLGS IKFGLKGAFD HQSPPENFSS EYDVMKPPSN 300 PNSTVSSGVY KLEFGKTIDV ILQNANALNA NVSEIHPWHL HGHDFWVLGY GEGKFSEEKH 360 SKNLNLKNPP LRNTVVIFPY GWTAIRFVTD NPGVWAFHCH IEPHLHMGMG VIFAESVERI 420 KNIPQAAIGC GMTAKMVMNN SHT* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03389 | laccase | 2.0e-51 | 5 | 413 | 438 | + laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. | ||
| TIGR03390 | ascorbOXfungal | 2.0e-52 | 9 | 413 | 439 | + L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized. | ||
| PLN02604 | PLN02604 | 2.0e-168 | 1 | 433 | 437 | + oxidoreductase | ||
| TIGR03388 | ascorbase | 0 | 1 | 433 | 436 | + L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. | ||
| PLN02191 | PLN02191 | 0 | 1 | 439 | 442 | + L-ascorbate oxidase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0016491 | oxidoreductase activity |
| 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 |
| EMBL | CAN82127.1 | 0 | 1 | 440 | 114 | 554 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002275678.1 | 0 | 1 | 440 | 137 | 577 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299782.1 | 0 | 1 | 442 | 120 | 564 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002312838.1 | 0 | 1 | 438 | 150 | 591 | l-ascorbate oxidase precursor [Populus trichocarpa] |
| RefSeq | XP_002530197.1 | 0 | 1 | 441 | 146 | 587 | l-ascorbate oxidase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1asq_B | 0 | 1 | 440 | 109 | 548 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 1asq_A | 0 | 1 | 440 | 109 | 548 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 1asp_B | 0 | 1 | 440 | 109 | 548 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 1asp_A | 0 | 1 | 440 | 109 | 548 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 1aso_B | 0 | 1 | 440 | 109 | 548 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DT751934 | 281 | 164 | 444 | 0 |
| DT732286 | 249 | 1 | 249 | 0 |
| DR923415 | 236 | 1 | 236 | 0 |
| DY305215 | 308 | 131 | 437 | 0 |
| DR938387 | 222 | 223 | 444 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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