| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s1_590V6.1 |
| Family | AA1 |
| Protein Properties | Length: 560 Molecular Weight: 61799.6 Isoelectric Point: 6.8197 |
| Chromosome | Chromosome/Scaffold: 1 Start: 3415264 End: 3417606 |
| Description | Plant L-ascorbate oxidase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA1 | 66 | 397 | 0 |
| FHWHGIHQTTTPFFDGAAYVSQCPINPGETFTYRFTVERAGTYFYHGHFGMQRAGGLFGSLIVSISLHKEPFAYDGEHSIILTDWWHKSIYEQQLGLTSI PFRFVGEPQSLLIQGRGSYNCTGLAGVAPGSLNCIVCNSTNPLCAPHVLPVMPGKTYRLRIASVASLSSLNFILEGHTLTVVQADGRYVKPFQVDNLNVY SGQSYDVLFTTNKEPSRNFWAAVNVRGRKMSTPTGLAILQYLPNPATLVPLTPTPVSPAWNDTAASVAQAKMILAKFGYEQAPPLKPDRTVTILGTQNMV DGHIKWALNNISHVARPTPVLAALKYNIRGAF | |||
| Full Sequence |
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| Protein Sequence Length: 560 Download |
| MVMLIAEAAV VKYDWTVDYI TASPDCVEKL VLSVNNQFPS PTIHAMEGDT LVVRVTNAIP 60 TEGVVFHWHG IHQTTTPFFD GAAYVSQCPI NPGETFTYRF TVERAGTYFY HGHFGMQRAG 120 GLFGSLIVSI SLHKEPFAYD GEHSIILTDW WHKSIYEQQL GLTSIPFRFV GEPQSLLIQG 180 RGSYNCTGLA GVAPGSLNCI VCNSTNPLCA PHVLPVMPGK TYRLRIASVA SLSSLNFILE 240 GHTLTVVQAD GRYVKPFQVD NLNVYSGQSY DVLFTTNKEP SRNFWAAVNV RGRKMSTPTG 300 LAILQYLPNP ATLVPLTPTP VSPAWNDTAA SVAQAKMILA KFGYEQAPPL KPDRTVTILG 360 TQNMVDGHIK WALNNISHVA RPTPVLAALK YNIRGAFDSE PPPDFPIKDY DVFAPPPTNY 420 RNATSGSPVY VFTKDSVVDI IVQNANTLTP NNSEIHPWHL HGHDFWILGY GEGQFDPEKD 480 PAFFNLVDPP VRNTVAVFPY GWVVIRFIAN NPGAWPFHCH IEPHFHMGMG TVFAEGIEHI 540 PELPTQTLGC GLTKRLMRL* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR03390 | ascorbOXfungal | 2.0e-84 | 26 | 536 | 538 | + 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. | ||
| TIGR03389 | laccase | 7.0e-103 | 8 | 533 | 559 | + 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. | ||
| TIGR03388 | ascorbase | 0 | 10 | 553 | 546 | + 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. | ||
| PLN02604 | PLN02604 | 0 | 5 | 555 | 553 | + oxidoreductase | ||
| PLN02191 | PLN02191 | 0 | 6 | 557 | 553 | + 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 |
| GenBank | ABR16553.1 | 0 | 13 | 557 | 31 | 573 | unknown [Picea sitchensis] |
| RefSeq | XP_001751352.1 | 0 | 1 | 559 | 1 | 559 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001763272.1 | 0 | 1 | 555 | 19 | 572 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001781653.1 | 0 | 1 | 557 | 1 | 560 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002530197.1 | 0 | 13 | 555 | 43 | 581 | 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 | 8 | 557 | 1 | 545 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 1asq_A | 0 | 8 | 557 | 1 | 545 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 1asp_B | 0 | 8 | 557 | 1 | 545 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 1asp_A | 0 | 8 | 557 | 1 | 545 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 1aso_B | 0 | 8 | 557 | 1 | 545 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO584787 | 558 | 12 | 552 | 0 |
| FC354424 | 265 | 294 | 557 | 0 |
| DW481317 | 296 | 13 | 306 | 0 |
| JG587746 | 286 | 6 | 290 | 0 |
| JG721307 | 270 | 5 | 274 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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