| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10021381m |
| Family | AA2 |
| Protein Properties | Length: 253 Molecular Weight: 28231.2 Isoelectric Point: 6.0491 |
| Chromosome | Chromosome/Scaffold: 13 Start: 6450441 End: 6452291 |
| Description | ascorbate peroxidase 2 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 24 | 245 | 0 |
| RGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPYGTIRHPQELAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKV EPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGPWTQNPLIFDNSYFKEILSGEKEGLLQLPTDKALLQDPLFRPLVERY AADEDAFFEDYTEAHLKLSELG | |||
| Full Sequence |
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| Protein Sequence Length: 253 Download |
| MVKSYPEVTE DYKKAIQRCK RKLRGLIAEK HCAPIVLRLA WHSAGTFDVK TKTGGPYGTI 60 RHPQELAHDA NNGLDIAVRL LDPIKELFPI LSYADFYQLA GVVAVEITGG PEIPFHPGRL 120 DKVEPPPEGR LPQATKGVDH LRDVFGRMGL NDKDIVALSG GHTLGRCHKE RSGFEGPWTQ 180 NPLIFDNSYF KEILSGEKEG LLQLPTDKAL LQDPLFRPLV ERYAADEDAF FEDYTEAHLK 240 LSELGFAENE KE* 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 6.0e-68 | 20 | 243 | 252 | + 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-142 | 6 | 246 | 241 | + L-ascorbate peroxidase | ||
| PLN02364 | PLN02364 | 8.0e-145 | 1 | 246 | 247 | + L-ascorbate peroxidase 1 | ||
| cd00691 | ascorbate_peroxidase | 4.0e-152 | 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 | 6.0e-174 | 3 | 250 | 248 | + 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 | AAF23294.1 | 0 | 3 | 245 | 4 | 246 | AC016661_19 putative ascorbate peroxidase [Arabidopsis thaliana] |
| GenBank | ABE65932.1 | 0 | 3 | 250 | 4 | 251 | L-ascorbate peroxidase 1b [Arabidopsis thaliana] |
| GenBank | ABK28551.1 | 0 | 3 | 250 | 4 | 251 | unknown [Arabidopsis thaliana] |
| EMBL | CAA56340.1 | 0 | 3 | 250 | 4 | 251 | ascorbate peroxidase [Arabidopsis thaliana] |
| RefSeq | NP_187575.2 | 0 | 3 | 250 | 4 | 251 | APX2 (ASCORBATE PEROXIDASE 2); L-ascorbate peroxidase [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1apx_D | 0 | 3 | 248 | 2 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 0 | 3 | 248 | 2 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 0 | 3 | 248 | 2 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 0 | 3 | 248 | 2 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 2xj6_A | 0 | 3 | 248 | 2 | 248 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EX290101 | 250 | 1 | 250 | 0 |
| EX276749 | 250 | 1 | 250 | 0 |
| EX291544 | 250 | 1 | 250 | 0 |
| EX259973 | 250 | 1 | 250 | 0 |
| EX264110 | 250 | 1 | 250 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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