| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01025551001 |
| Family | AA2 |
| Protein Properties | Length: 254 Molecular Weight: 27985.8 Isoelectric Point: 5.4005 |
| Chromosome | Chromosome/Scaffold: 8 Start: 14111050 End: 14113960 |
| Description | ascorbate peroxidase 2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 27 | 245 | 0 |
| IAEKKCAPLMLRLAWHSAGTYDVKTKTGGPFGTMKHPEELAHEANNGLDIAVRLLEPIKEQFPILSYGDFYQLAGVVAVEVTGGPEIPFHPGRQDKSEPP PEGRLPNATKGSDHLRDVFGHMGLSDKDIVALSGGHTLGRCHKERSGFEGPWTTNPLIFDNSYFKELLSGEKEGLIQLPSDKALLEDPVFRPLVEKYAMD EDAFFADYAEAHLKLSEVG | |||
| Full Sequence |
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| Protein Sequence Length: 254 Download |
| MGKAYPIVSE EYQKAVEKCK RKLRGFIAEK KCAPLMLRLA WHSAGTYDVK TKTGGPFGTM 60 KHPEELAHEA NNGLDIAVRL LEPIKEQFPI LSYGDFYQLA GVVAVEVTGG PEIPFHPGRQ 120 DKSEPPPEGR LPNATKGSDH LRDVFGHMGL SDKDIVALSG GHTLGRCHKE RSGFEGPWTT 180 NPLIFDNSYF KELLSGEKEG LIQLPSDKAL LEDPVFRPLV EKYAMDEDAF FADYAEAHLK 240 LSEVGFADAE EQG* 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 4.0e-57 | 20 | 222 | 231 | + Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase. | ||
| PLN02608 | PLN02608 | 3.0e-131 | 4 | 246 | 243 | + L-ascorbate peroxidase | ||
| PLN02364 | PLN02364 | 9.0e-134 | 1 | 249 | 250 | + L-ascorbate peroxidase 1 | ||
| cd00691 | ascorbate_peroxidase | 7.0e-141 | 5 | 249 | 253 | + Ascorbate peroxidases and cytochrome C peroxidases. Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water. | ||
| PLN02879 | PLN02879 | 3.0e-145 | 1 | 250 | 250 | + L-ascorbate peroxidase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004601 | peroxidase activity |
| GO:0006979 | response to oxidative stress |
| GO:0020037 | heme 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 | ABX79340.1 | 0 | 1 | 253 | 1 | 253 | cytosolic ascorbate peroxidase [Vitis vinifera] |
| GenBank | ACF06591.1 | 0 | 1 | 249 | 1 | 249 | cytosolic ascorbate peroxidase [Elaeis guineensis] |
| GenBank | ACM17463.1 | 0 | 1 | 250 | 1 | 250 | ascorbate peroxidase [Citrus maxima] |
| EMBL | CAN59923.1 | 0 | 1 | 246 | 1 | 246 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI32625.1 | 0 | 1 | 253 | 1 | 253 | unnamed protein product [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2xj6_A | 0 | 2 | 249 | 1 | 249 | A Chain A, Crystal Structure Of A Putative Ubiquitin-Conjugating Enzyme E2 From Toxoplasma Gondii |
| PDB | 2xih_A | 0 | 2 | 249 | 1 | 249 | A Chain A, Crystal Structure Of A Putative Ubiquitin-Conjugating Enzyme E2 From Toxoplasma Gondii |
| PDB | 2xif_A | 0 | 2 | 249 | 1 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2xi6_A | 0 | 2 | 249 | 1 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2vcf_X | 0 | 3 | 251 | 14 | 263 | X Chain X, Structure Of Isoniazid (Inh) Bound To Cytosolic Soybean Ascorbate Peroxidase |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| L-ascorbate degradation III | RXN-12440 | EC-1.11.1.11 | L-ascorbate peroxidase |
| L-ascorbate degradation V | RXN-12440 | EC-1.11.1.11 | L-ascorbate peroxidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FQ439280 | 254 | 1 | 254 | 0 |
| CB969798 | 254 | 1 | 254 | 0 |
| EC961857 | 222 | 1 | 222 | 0 |
| CV100504 | 217 | 1 | 217 | 0 |
| EX290101 | 250 | 1 | 250 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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