y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.004G227200.4 |
Family | AA2 |
Protein Properties | Length: 126 Molecular Weight: 13653.8 Isoelectric Point: 8.7048 |
Chromosome | Chromosome/Scaffold: 04 Start: 56158166 End: 56159057 |
Description | ascorbate peroxidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 18 | 120 | 1e-31 |
KAKRKLRALIAEKNCAPLMLRLAWHSAGTFDVKTKTGGPFGTMKQPAELAHAANNGLDIAVRLLEPIKEQFPILSYADFYQLAGVAAVEVTGGPEVPFHP GRE |
Full Sequence |
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Protein Sequence Length: 126 Download |
MTKCYPTVSE EYQNAVQKAK RKLRALIAEK NCAPLMLRLA WHSAGTFDVK TKTGGPFGTM 60 KQPAELAHAA NNGLDIAVRL LEPIKEQFPI LSYADFYQLA GVAAVEVTGG PEVPFHPGRE 120 VSLNL* 180 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 4.0e-26 | 17 | 125 | 116 | + 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-58 | 6 | 122 | 117 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 9.0e-62 | 5 | 119 | 116 | + 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. | ||
PLN02364 | PLN02364 | 9.0e-65 | 1 | 120 | 120 | + L-ascorbate peroxidase 1 | ||
PLN02879 | PLN02879 | 3.0e-69 | 1 | 119 | 119 | + 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 | AAB82778.1 | 0 | 1 | 120 | 1 | 120 | ripening-associated protein [Musa acuminata AAA Group] |
GenBank | AAC08576.1 | 0 | 1 | 120 | 1 | 120 | ascorbate peroxidase [Zantedeschia aethiopica] |
GenBank | AAL08496.1 | 0 | 3 | 120 | 4 | 121 | ascorbate peroxidase [Hordeum vulgare subsp. vulgare] |
GenBank | AAN60070.1 | 0 | 1 | 120 | 1 | 120 | cytosolic ascorbate peroxidase [Retama raetam] |
RefSeq | XP_002326165.1 | 0 | 1 | 119 | 1 | 119 | 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 | 1apx_D | 0 | 3 | 120 | 2 | 119 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_C | 0 | 3 | 120 | 2 | 119 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_B | 0 | 3 | 120 | 2 | 119 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_A | 0 | 3 | 120 | 2 | 119 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xj6_A | 0 | 3 | 120 | 2 | 119 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DW517360 | 126 | 1 | 126 | 0 |
EV481817 | 120 | 1 | 120 | 0 |
EV494819 | 120 | 1 | 120 | 0 |
CO096238 | 120 | 1 | 120 | 0 |
EV489274 | 120 | 1 | 120 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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