y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_014643m |
Family | AA2 |
Protein Properties | Length: 251 Molecular Weight: 27669.3 Isoelectric Point: 5.1915 |
Chromosome | Chromosome/Scaffold: 00506 Start: 148152 End: 151496 |
Description | ascorbate peroxidase 1 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 28 | 246 | 0 |
AEKGCAPLMLRIAWHSAGTYDVKTNTGGPFGTMRHAAEQGHAANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVVAVEITGGPDIPFHPGREDKPEPPP EGRLPNATKGADHLREVFGKTMGLTDKDIVVLSGGHTLGRCHKERSGFEGPWTPNPLIFDNSFFQVLLDEPTEDLLQLPTDSVLVTDPVFRPYVEKYAAD EEAFFADYAESHMKLSELG |
Full Sequence |
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Protein Sequence Length: 251 Download |
MPKNYPKVSE EYQKAIDKAR RKLRGFIAEK GCAPLMLRIA WHSAGTYDVK TNTGGPFGTM 60 RHAAEQGHAA NNGLDIAVRL LEPIKEQFPI LSYADFYQLA GVVAVEITGG PDIPFHPGRE 120 DKPEPPPEGR LPNATKGADH LREVFGKTMG LTDKDIVVLS GGHTLGRCHK ERSGFEGPWT 180 PNPLIFDNSF FQVLLDEPTE DLLQLPTDSV LVTDPVFRPY VEKYAADEEA FFADYAESHM 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 | 9.0e-51 | 17 | 244 | 256 | + 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 | 6.0e-127 | 6 | 247 | 242 | + L-ascorbate peroxidase | ||
PLN02879 | PLN02879 | 1.0e-127 | 3 | 249 | 247 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 2.0e-129 | 1 | 250 | 250 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 1.0e-139 | 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 | AAO14118.1 | 0 | 1 | 250 | 1 | 250 | AF457210_1 ascorbate peroxidase [Hevea brasiliensis] |
GenBank | AAX84679.1 | 0 | 1 | 250 | 1 | 250 | ascorbate peroxidase APX2 [Manihot esculenta] |
GenBank | ABP87792.1 | 0 | 1 | 250 | 1 | 250 | ascorbate peroxidase [Malus x domestica] |
GenBank | ACO57439.1 | 0 | 1 | 250 | 1 | 249 | cytosolic ascorbate peroxidase [Elaeis oleifera] |
GenBank | ACV50426.1 | 0 | 1 | 250 | 1 | 250 | cytosolic ascorbate peroxidase-1 [Jatropha curcas] |
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 | 1apx_D | 0 | 3 | 250 | 2 | 249 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_C | 0 | 3 | 250 | 2 | 249 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_B | 0 | 3 | 250 | 2 | 249 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_A | 0 | 3 | 250 | 2 | 249 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xj6_A | 0 | 3 | 250 | 2 | 249 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
Metabolic Pathways | |||
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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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DV454843 | 248 | 1 | 248 | 0 |
DV456138 | 251 | 1 | 251 | 0 |
DV446757 | 248 | 1 | 248 | 0 |
DV445756 | 248 | 1 | 248 | 0 |
DV445199 | 243 | 1 | 243 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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