| Basic Information | |
|---|---|
| Species | Eucalyptus grandis |
| Cazyme ID | Eucgr.I01408.1 |
| Family | AA2 |
| Protein Properties | Length: 288 Molecular Weight: 31522.9 Isoelectric Point: 7.1948 |
| Chromosome | Chromosome/Scaffold: 9 Start: 24533365 End: 24537991 |
| Description | ascorbate peroxidase 3 |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 25 | 243 | 0 |
| IAYKNCAPIMLRLAWHDAGTYDARTKTGGPTGSIRNEEEYSHGANAGLKIALDFCEDVKSKCPRITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSRVSP NEGRLPDANQGPPHLRDIFYRMGLSDKDIVALSGAHTLGRAHPERSGFDGPWTQEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPAFRPYVELYAKD EDAFFRDYVISHKKLSELG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 288 Download |
| MALPVVDTEY LKEIDKARRH LRALIAYKNC APIMLRLAWH DAGTYDARTK TGGPTGSIRN 60 EEEYSHGANA GLKIALDFCE DVKSKCPRIT YADLYQLAGV VAVEVTGGPT IDFVPGRKDS 120 RVSPNEGRLP DANQGPPHLR DIFYRMGLSD KDIVALSGAH TLGRAHPERS GFDGPWTQEP 180 LKFDNSYFVE LLKGESEGLL KLPTDKALLE DPAFRPYVEL YAKDEDAFFR DYVISHKKLS 240 ELGFTPSSSG SKTVANGAVL AQGAVGVAVA AAVVILSYFY EVRKKMK* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam00141 | peroxidase | 1.0e-52 | 17 | 224 | 218 | + Peroxidase. |
| PLN02364 | PLN02364 | 2.0e-99 | 4 | 244 | 242 | + L-ascorbate peroxidase 1 |
| PLN02879 | PLN02879 | 5.0e-102 | 2 | 244 | 243 | + L-ascorbate peroxidase |
| cd00691 | ascorbate_peroxidase | 3.0e-143 | 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 | 287 | 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 - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ABA10744.1 | 0 | 1 | 287 | 1 | 287 | cytosolic ascorbate peroxidase isoform 4 [Solanum lycopersicum] |
| GenBank | ACT87980.1 | 0 | 1 | 255 | 1 | 255 | ascorbate peroxidase [Jatropha curcas] |
| RefSeq | NP_195226.1 | 0 | 1 | 287 | 1 | 287 | APX3 (ASCORBATE PEROXIDASE 3); L-ascorbate peroxidase [Arabidopsis thaliana] |
| RefSeq | XP_002312965.1 | 0 | 1 | 287 | 1 | 286 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002530823.1 | 0 | 1 | 287 | 1 | 288 | L-ascorbate peroxidase 1, cytosolic, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1apx_D | 0 | 4 | 244 | 5 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 0 | 4 | 244 | 5 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 0 | 4 | 244 | 5 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 0 | 4 | 244 | 5 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 2vcf_X | 0 | 4 | 244 | 17 | 258 | X Chain X, Structure Of Isoniazid (Inh) Bound To Cytosolic Soybean Ascorbate Peroxidase |
