y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.011G071300.1 |
Family | AA2 |
Protein Properties | Length: 251 Molecular Weight: 27075.7 Isoelectric Point: 5.6303 |
Chromosome | Chromosome/Scaffold: 11 Start: 6378762 End: 6381275 |
Description | ascorbate peroxidase 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 27 | 246 | 0 |
IAEKRCAPLMLRLAWHSAGTFDVSTKTGGPFGTIKHPSELAHGANNGLDIAVRLLEPLKAEFPILSYADFYQLAGVVGVEVTGGPEVPFYPGREDKPEPP PEGRLPDATKGSDHLRDVFGKAMGLSDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFKELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAA DEDAFFADYAVAHQKLSELG |
Full Sequence |
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Protein Sequence Length: 251 Download |
MGKSYPSVSA DYQKAIEKAK RKLRGFIAEK RCAPLMLRLA WHSAGTFDVS TKTGGPFGTI 60 KHPSELAHGA NNGLDIAVRL LEPLKAEFPI LSYADFYQLA GVVGVEVTGG PEVPFYPGRE 120 DKPEPPPEGR LPDATKGSDH LRDVFGKAMG LSDQDIVALS GGHTIGAAHK ERSGFEGPWT 180 SNPLIFDNSY FKELLSGEKE GLLQLPSDKA LLSDPVFRPL VDKYAADEDA FFADYAVAHQ 240 KLSELGFAEA * 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 2.0e-39 | 17 | 221 | 233 | + 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-106 | 1 | 250 | 250 | + L-ascorbate peroxidase 1 | ||
PLN02608 | PLN02608 | 4.0e-106 | 6 | 247 | 242 | + L-ascorbate peroxidase | ||
PLN02879 | PLN02879 | 4.0e-109 | 1 | 249 | 249 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 3.0e-111 | 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAA61779.1 | 0 | 1 | 250 | 1 | 250 | ascorbate peroxidase [Glycine max] |
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] |
DDBJ | BAC92740.1 | 0 | 1 | 250 | 1 | 250 | cytosolic ascorbate peroxidase 2 [Glycine max] |
Annotations - PDB Download unfiltered results here | |||||||
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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, The Crystal Structure Of A Cyanogenic Beta-Glucosidase From White Clover (Trifolium Repens L.), A Family 1 Glycosyl-Hydrolase |
PDB | 2xih_A | 0 | 2 | 250 | 1 | 249 | A Chain A, The Crystal Structure Of A Cyanogenic Beta-Glucosidase From White Clover (Trifolium Repens L.), A Family 1 Glycosyl-Hydrolase |
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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE698025 | 251 | 1 | 251 | 0 |
FE698027 | 251 | 1 | 251 | 0 |
GW902154 | 251 | 1 | 251 | 0 |
GW889023 | 251 | 1 | 251 | 0 |
HO777306 | 251 | 1 | 251 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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