| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G004211_T01 |
| Family | AA2 |
| Protein Properties | Length: 291 Molecular Weight: 32072.4 Isoelectric Point: 8.0038 |
| Chromosome | Chromosome/Scaffold: 10 Start: 101005463 End: 101007288 |
| Description | ascorbate peroxidase 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 23 | 243 | 0 |
| ALVASKNCAPIMLRLAWHDAGTYDAKTNTGGPNGSIRFPQEYSHSSNAGIKIAIDLLEPVKQKHPKITYADLYQLAGVVAVEVTGGPTVDFVPGRKDSSI CPEEGRLPDARRGASHLRQVFYRMGLSDRDIVALSGGHTLGRAHRERTGFDGPWTRDPLKFDNSYFLELLKGDSEGLLKLPTDKVLVEDPEFRQHVQLYA KDEDAFFRDYAESHKKLSELG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 291 Download |
| MSAPLVDAEY MAEIERARRD LRALVASKNC APIMLRLAWH DAGTYDAKTN TGGPNGSIRF 60 PQEYSHSSNA GIKIAIDLLE PVKQKHPKIT YADLYQLAGV VAVEVTGGPT VDFVPGRKDS 120 SICPEEGRLP DARRGASHLR QVFYRMGLSD RDIVALSGGH TLGRAHRERT GFDGPWTRDP 180 LKFDNSYFLE LLKGDSEGLL KLPTDKVLVE DPEFRQHVQL YAKDEDAFFR DYAESHKKLS 240 ELGFTPPRSC LSSRSANKHK SLLVQAAAGL AVATAVVAWA YLCESNNKFI * 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 3.0e-57 | 15 | 241 | 255 | + 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 | 7.0e-107 | 4 | 244 | 242 | + L-ascorbate peroxidase 1 | ||
| PLN02879 | PLN02879 | 2.0e-112 | 2 | 244 | 243 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 3.0e-159 | 3 | 247 | 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. | ||
| PLN02608 | PLN02608 | 0 | 1 | 257 | 257 | + 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 | ACR37850.1 | 0 | 1 | 247 | 1 | 247 | unknown [Zea mays] |
| RefSeq | NP_001052271.1 | 0 | 2 | 289 | 3 | 290 | Os04g0223300 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001148710.1 | 0 | 1 | 290 | 1 | 290 | APx3 - Peroxisomal Ascorbate Peroxidase [Zea mays] |
| Swiss-Prot | Q01MI9 | 0 | 2 | 289 | 3 | 290 | APX3_ORYSI RecName: Full=Probable L-ascorbate peroxidase 3; AltName: Full=OsAPx03 |
| RefSeq | XP_002446119.1 | 0 | 1 | 290 | 1 | 290 | hypothetical protein SORBIDRAFT_06g001970 [Sorghum bicolor] |
| 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 | 244 | 3 | 246 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 2xih_A | 0 | 2 | 244 | 3 | 246 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 2xif_A | 0 | 2 | 244 | 3 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2xi6_A | 0 | 2 | 244 | 3 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2vcf_X | 0 | 2 | 244 | 15 | 258 | X Chain X, Structure Of Isoniazid (Inh) Bound To Cytosolic Soybean Ascorbate Peroxidase |
