| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma12g07780.3 |
| Family | AA2 |
| Protein Properties | Length: 251 Molecular Weight: 27125.7 Isoelectric Point: 5.8662 |
| Chromosome | Chromosome/Scaffold: 12 Start: 5387682 End: 5390392 |
| Description | ascorbate peroxidase 1 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 22 | 246 | 0 |
| KLRGFIAEKRCAPLMLRLAWHSAGTYDVSSKTGGPFGTIKHPSELAHGANNGLDIAVRLLEPLKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGRED KPEPPPEGRLPDATKGSDHLRDVFGKAMGLSDRDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFKELLSGEKEGLLQLPSDKALLSDPVFRPLV EKYASDEDAFFADYAEAHQKLSELG | |||
| Full Sequence |
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| Protein Sequence Length: 251 Download |
| MGKSYPTVSA DYQKAVEKAK KKLRGFIAEK RCAPLMLRLA WHSAGTYDVS SKTGGPFGTI 60 KHPSELAHGA NNGLDIAVRL LEPLKAEFPI LSYADFYQLA GVVAVEVTGG PEVPFHPGRE 120 DKPEPPPEGR LPDATKGSDH LRDVFGKAMG LSDRDIVALS GGHTIGAAHK ERSGFEGPWT 180 SNPLIFDNSY FKELLSGEKE GLLQLPSDKA LLSDPVFRPL VEKYASDEDA FFADYAEAHQ 240 KLSELGFAEA * 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 8.0e-50 | 17 | 223 | 235 | + 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 | 8.0e-118 | 6 | 247 | 242 | + L-ascorbate peroxidase | ||
| PLN02364 | PLN02364 | 1.0e-120 | 1 | 250 | 250 | + L-ascorbate peroxidase 1 | ||
| PLN02879 | PLN02879 | 8.0e-122 | 1 | 249 | 249 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 2.0e-126 | 5 | 250 | 254 | + 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 | AAB01221.1 | 0 | 1 | 250 | 1 | 250 | ascorbate peroxidase 2 [Glycine max] |
| GenBank | AAB03844.1 | 0 | 1 | 250 | 1 | 250 | cytosolic ascorbate peroxidase [Vigna unguiculata] |
| GenBank | AAD20022.1 | 0 | 1 | 250 | 1 | 250 | ascorbate peroxidase [Glycine max] |
| GenBank | ACU19647.1 | 0 | 1 | 250 | 1 | 250 | unknown [Glycine max] |
| DDBJ | BAC92740.1 | 0 | 1 | 250 | 1 | 250 | cytosolic ascorbate peroxidase 2 [Glycine max] |
| 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 | 250 | 1 | 249 | A Chain A, Crystal Structure Of Choline Oxidase Reveals Insights Into The Catalytic Mechanism |
| PDB | 2xih_A | 0 | 2 | 250 | 1 | 249 | A Chain A, Crystal Structure Of Choline Oxidase Reveals Insights Into The Catalytic Mechanism |
| PDB | 2xif_A | 0 | 2 | 250 | 1 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2xi6_A | 0 | 2 | 250 | 1 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
| PDB | 2y6b_A | 0 | 2 | 250 | 1 | 249 | A Chain A, Ascorbate Peroxidase R38k Mutant |
| 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 |
| HO760901 | 251 | 1 | 251 | 0 |
| GR827589 | 249 | 1 | 249 | 0 |
| EH262513 | 251 | 1 | 251 | 0 |
| FG935819 | 248 | 1 | 248 | 0 |
| HO777306 | 251 | 1 | 251 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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