y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.009G015400.1 |
Family | AA2 |
Protein Properties | Length: 252 Molecular Weight: 27400.4 Isoelectric Point: 7.1645 |
Chromosome | Chromosome/Scaffold: 09 Start: 2615414 End: 2618311 |
Description | ascorbate peroxidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 20 | 224 | 0 |
KKKLRSLIAEKSCAPLMLRLAWHSAGTFDVKTKTGGPFGTMRYSAELAHGANNGLDIAVRLLESIKEQFPILSYADFYQLAGVVGVEITGGPEVPFHPGR EDKPEPPPEGRLPDATKGSDHLRDVFGHMGLSDKDIVALSGGHTLGRCHKERSGFEGPWTANPLIFDNSYFKELLSGEKEGLLQLPSDKALLSDPIFRPY VDKYA |
Full Sequence |
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Protein Sequence Length: 252 Download |
MTKNYPTVSE EYSKAVEKAK KKLRSLIAEK SCAPLMLRLA WHSAGTFDVK TKTGGPFGTM 60 RYSAELAHGA NNGLDIAVRL LESIKEQFPI LSYADFYQLA GVVGVEITGG PEVPFHPGRE 120 DKPEPPPEGR LPDATKGSDH LRDVFGHMGL SDKDIVALSG GHTLGRCHKE RSGFEGPWTA 180 NPLIFDNSYF KELLSGEKEG LLQLPSDKAL LSDPIFRPYV DKYAAVCTKN IICCASGACQ 240 IHEKLLVSCC C* 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 | 3.0e-52 | 17 | 226 | 238 | + 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 | 3.0e-120 | 6 | 224 | 219 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 2.0e-126 | 1 | 225 | 226 | + L-ascorbate peroxidase 1 | ||
PLN02879 | PLN02879 | 4.0e-129 | 1 | 225 | 225 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 2.0e-129 | 5 | 225 | 229 | + 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 | ACF06591.1 | 0 | 1 | 225 | 1 | 225 | cytosolic ascorbate peroxidase [Elaeis guineensis] |
EMBL | CBI32625.1 | 0 | 1 | 224 | 1 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001152249.1 | 0 | 1 | 225 | 1 | 226 | APx1 - Cytosolic Ascorbate Peroxidase [Zea mays] |
RefSeq | NP_001152746.1 | 0 | 1 | 225 | 1 | 226 | ascorbate peroxidase [Zea mays] |
RefSeq | XP_002313506.1 | 0 | 1 | 225 | 1 | 225 | predicted protein [Populus trichocarpa] |
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 | 2vcf_X | 0 | 3 | 225 | 14 | 237 | X Chain X, Structure Of Isoniazid (Inh) Bound To Cytosolic Soybean Ascorbate Peroxidase |
PDB | 2xj6_A | 0 | 3 | 225 | 2 | 225 | X Chain X, Structure Of Isoniazid (Inh) Bound To Cytosolic Soybean Ascorbate Peroxidase |
PDB | 2xih_A | 0 | 3 | 225 | 2 | 225 | X Chain X, Structure Of Isoniazid (Inh) Bound To Cytosolic Soybean Ascorbate Peroxidase |
PDB | 2xif_A | 0 | 3 | 225 | 2 | 225 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 3 | 225 | 2 | 225 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
ascorbate glutathione cycle | RXN-3521 | - | L-ascorbate peroxidase |
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 |
DT501049 | 225 | 1 | 225 | 0 |
DT472881 | 225 | 1 | 225 | 0 |
DT507358 | 225 | 1 | 225 | 0 |
DT473981 | 225 | 1 | 225 | 0 |
DT474088 | 225 | 1 | 225 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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