Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.006G132200.1 |
Family | AA2 |
Protein Properties | Length: 269 Molecular Weight: 29770.5 Isoelectric Point: 9.3991 |
Chromosome | Chromosome/Scaffold: 06 Start: 10848399 End: 10851682 |
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 | 25 | 165 | 0 |
GLIAEKHCAPLMLRLAWHSAGTFDVHTKTGGPFGTIRHPDELAHGANNGLDIAIRLLEPIKEQFPILSYADFYQLAGVVAVEVTGGPEIPFHPGRPDKSD PPPEGRLPDATKGSDHLRDVFGHMGLSDTDIVALSGGHTLV |
Full Sequence |
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Protein Sequence Length: 269 Download |
MGKSYPTVSE EYQKAVEKCK RKLRGLIAEK HCAPLMLRLA WHSAGTFDVH TKTGGPFGTI 60 RHPDELAHGA NNGLDIAIRL LEPIKEQFPI LSYADFYQLA GVVAVEVTGG PEIPFHPGRP 120 DKSDPPPEGR LPDATKGSDH LRDVFGHMGL SDTDIVALSG GHTLVCSQTW NYVKNFLLIL 180 FCLCTIGVCT YIYRGGAIRS VLDSRDPGPP THLFSTTPIS RNSSVERKKV LSSFHQTKLF 240 WRIQSSVPLL KTMLKMRMHS LQIIQKLI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 3.0e-46 | 26 | 163 | 147 | + Peroxidase. | ||
PLN02608 | PLN02608 | 3.0e-90 | 6 | 164 | 159 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 1.0e-93 | 1 | 164 | 165 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 7.0e-98 | 5 | 164 | 164 | + 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 | 1.0e-103 | 1 | 164 | 164 | + 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 | 3 | 164 | 4 | 165 | cytosolic ascorbate peroxidase [Dimocarpus longan] |
GenBank | ABZ79406.1 | 0 | 3 | 164 | 4 | 165 | ascorbate peroxidase [Litchi chinensis] |
GenBank | ACM17463.1 | 0 | 1 | 164 | 1 | 164 | ascorbate peroxidase [Citrus maxima] |
RefSeq | XP_002322851.1 | 0 | 1 | 164 | 1 | 164 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002326165.1 | 0 | 1 | 164 | 1 | 164 | 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 | 2 | 164 | 1 | 164 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_C | 0 | 2 | 164 | 1 | 164 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_B | 0 | 2 | 164 | 1 | 164 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_A | 0 | 2 | 164 | 1 | 164 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xj6_A | 0 | 2 | 168 | 1 | 168 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
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 |