Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.A01180.1 |
Family | AA2 |
Protein Properties | Length: 250 Molecular Weight: 27459.2 Isoelectric Point: 6.5133 |
Chromosome | Chromosome/Scaffold: 1 Start: 18307831 End: 18311466 |
Description | ascorbate peroxidase 2 |
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 | 245 | 0 |
IAEKHCAPIVLRLAWHSAGTFDVQTKTGGPFGTIRHSAELAHEANNGLDIAVRLLEPIKAQFPILSYADFYQLAGVVAVEITGGPEIPFHPGRPDKNEPP PEGRLPEATKGSDHLRQVFGHMGLSDKDIVALSGGHTLGRCHKERSGFEGPWTTNPLIFDNSYFKELLSGDKEGLIKLPSDKALIEDPIFRPLVEKYAAD EDAFFADYEEAHLKLSELG |
Full Sequence |
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Protein Sequence Length: 250 Download |
MAKRYPNVSE EYRKAAAKCK RKLRGLIAEK HCAPIVLRLA WHSAGTFDVQ TKTGGPFGTI 60 RHSAELAHEA NNGLDIAVRL LEPIKAQFPI LSYADFYQLA GVVAVEITGG PEIPFHPGRP 120 DKNEPPPEGR LPEATKGSDH LRQVFGHMGL SDKDIVALSG GHTLGRCHKE RSGFEGPWTT 180 NPLIFDNSYF KELLSGDKEG LIKLPSDKAL IEDPIFRPLV EKYAADEDAF FADYEEAHLK 240 LSELGFADA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 5.0e-58 | 28 | 222 | 222 | + 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 | 7.0e-122 | 6 | 246 | 241 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 2.0e-123 | 1 | 249 | 250 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 1.0e-132 | 25 | 249 | 232 | + 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. | ||
PLN02879 | PLN02879 | 2.0e-136 | 3 | 248 | 246 | + L-ascorbate peroxidase |
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 | ABS50864.1 | 0 | 1 | 249 | 1 | 250 | cytosolic ascorbate peroxidase [Dimocarpus longan] |
GenBank | ABX79340.1 | 0 | 1 | 249 | 1 | 249 | cytosolic ascorbate peroxidase [Vitis vinifera] |
GenBank | ABZ79406.1 | 0 | 1 | 249 | 1 | 250 | ascorbate peroxidase [Litchi chinensis] |
GenBank | ACM17463.1 | 0 | 1 | 249 | 1 | 249 | ascorbate peroxidase [Citrus maxima] |
EMBL | CBI32625.1 | 0 | 1 | 249 | 1 | 249 | unnamed protein product [Vitis vinifera] |
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 | 3 | 249 | 2 | 249 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2xih_A | 0 | 3 | 249 | 2 | 249 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2xif_A | 0 | 3 | 249 | 2 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 3 | 249 | 2 | 249 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2ghk_X | 0 | 3 | 249 | 14 | 261 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
JK647738 | 220 | 1 | 220 | 0 |
CV195237 | 249 | 1 | 249 | 0 |
EX290101 | 249 | 1 | 249 | 0 |
EX276749 | 249 | 1 | 249 | 0 |
EX291544 | 249 | 1 | 249 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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