| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_028424m |
| Family | AA2 |
| Protein Properties | Length: 241 Molecular Weight: 26660.8 Isoelectric Point: 6.0528 |
| Chromosome | Chromosome/Scaffold: 03004 Start: 154 End: 2460 |
| Description | stromal ascorbate peroxidase |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 1 | 235 | 0 |
| VRLGWHDAGTYNKNIEEWPKRGGANGSIRFEVELKHGANAGLVNALNLLQPIKDKYSGVTYADLFQLASAIAIEEAGGPKIPMKYGRVDVSAPDDCPEEG RLPSAGPPKPADHLREVFYRMGLNDQDIVALSGAHTLGRSRPDRSGWGKPETKYTKSGPGEPGGQSWTAEWLKFDNSYFRDIKERKDEDLLVLPTDAVIF EDSSFKVYAEKYAADQKAFFKDYSEAHAKLSNLGA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 241 Download |
| VRLGWHDAGT YNKNIEEWPK RGGANGSIRF EVELKHGANA GLVNALNLLQ PIKDKYSGVT 60 YADLFQLASA IAIEEAGGPK IPMKYGRVDV SAPDDCPEEG RLPSAGPPKP ADHLREVFYR 120 MGLNDQDIVA LSGAHTLGRS RPDRSGWGKP ETKYTKSGPG EPGGQSWTAE WLKFDNSYFR 180 DIKERKDEDL LVLPTDAVIF EDSSFKVYAE KYAADQKAFF KDYSEAHAKL SNLGAKFDPP 240 Q 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 1.0e-42 | 1 | 232 | 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. | ||
| PLN02364 | PLN02364 | 5.0e-53 | 1 | 234 | 235 | + L-ascorbate peroxidase 1 | ||
| PLN02879 | PLN02879 | 6.0e-57 | 1 | 234 | 234 | + L-ascorbate peroxidase | ||
| PLN02608 | PLN02608 | 2.0e-80 | 1 | 240 | 240 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 5.0e-122 | 1 | 238 | 242 | + 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. | ||
| 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 | ACJ11732.1 | 0 | 1 | 241 | 137 | 377 | stromal ascorbate peroxidase [Gossypium hirsutum] |
| GenBank | ACT56518.1 | 0 | 1 | 241 | 103 | 343 | chloroplast stromal ascorbate peroxidase [Gossypium hirsutum] |
| RefSeq | XP_002300978.1 | 0 | 1 | 239 | 98 | 336 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002307442.1 | 0 | 1 | 241 | 29 | 269 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002520353.1 | 0 | 1 | 241 | 117 | 357 | Cytochrome c peroxidase, mitochondrial precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1iyn_A | 0 | 1 | 241 | 29 | 269 | A Chain A, Crystal Structure Of Chloroplastic Ascorbate Peroxidase From Tobacco Plants And Structural Insights For Its Instability |
| PDB | 1apx_D | 0 | 1 | 234 | 36 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 0 | 1 | 234 | 36 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 0 | 1 | 234 | 36 | 245 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 0 | 1 | 234 | 36 | 245 | A Chain A, Crystal Structure Of Recombinant 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 |
| FP031473 | 241 | 1 | 241 | 0 |
| EX262979 | 241 | 1 | 241 | 0 |
| HO779395 | 241 | 1 | 241 | 0 |
| HO283916 | 241 | 1 | 241 | 0 |
| JK987958 | 241 | 1 | 241 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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