| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 29602.m000217 |
| Family | AA2 |
| Protein Properties | Length: 288 Molecular Weight: 32059.6 Isoelectric Point: 7.6804 |
| Chromosome | Chromosome/Scaffold: 29602 Start: 103458 End: 113976 |
| Description | ascorbate peroxidase 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 24 | 243 | 0 |
| LIAYKNCAPIMLRLAWHDAGTYDKHTKTGGPNGSIRNEEEYSHGSNNGLKIALDFCEEVKAKHPRITYADLYQLAGVVAVEVTGGPSINFVPGRKDSKIS PREGRLPDAKQGPPHLRDIFHRMGLCDKDIVALSGGHTLGRAHPERSGFDGPWTKEPLKFDNSYFVELLKGETEGLLKLPTDKALLEDPEFRPYVELYAK DEEAFFKDYAESHKRLSELG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 288 Download |
| MSLPVVDTEY MKEIDKARRD LRALIAYKNC APIMLRLAWH DAGTYDKHTK TGGPNGSIRN 60 EEEYSHGSNN GLKIALDFCE EVKAKHPRIT YADLYQLAGV VAVEVTGGPS INFVPGRKDS 120 KISPREGRLP DAKQGPPHLR DIFHRMGLCD KDIVALSGGH TLGRAHPERS GFDGPWTKEP 180 LKFDNSYFVE LLKGETEGLL KLPTDKALLE DPEFRPYVEL YAKDEEAFFK DYAESHKRLS 240 ELGFTPSSSG SKVIAKDSVI LAQSAVGVAV AAAVVIFSYF YEVRKRMK |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam00141 | peroxidase | 2.0e-53 | 17 | 224 | 218 | + Peroxidase. |
| PLN02364 | PLN02364 | 3.0e-97 | 4 | 244 | 242 | + L-ascorbate peroxidase 1 |
| PLN02879 | PLN02879 | 5.0e-101 | 2 | 244 | 243 | + L-ascorbate peroxidase |
| cd00691 | ascorbate_peroxidase | 2.0e-148 | 4 | 246 | 251 | + 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. |
| PLN02608 | PLN02608 | 0 | 1 | 288 | 289 | + 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 - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2xj6_A | 0 | 2 | 245 | 3 | 247 | A Chain A, Crystal Structure Of An Indole-3-acetic Acid Amido Synthase From Vitis Vinifera Involved In Auxin Homeostasis |
| PDB | 2xih_A | 0 | 2 | 245 | 3 | 247 | A Chain A, Crystal Structure Of An Indole-3-acetic Acid Amido Synthase From Vitis Vinifera Involved In Auxin Homeostasis |
| PDB | 2xif_A | 0 | 2 | 245 | 3 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2xi6_A | 0 | 2 | 245 | 3 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2ghk_X | 0 | 2 | 245 | 15 | 259 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
