Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 478284 |
Family | AA2 |
Protein Properties | Length: 252 Molecular Weight: 28179.2 Isoelectric Point: 6.4269 |
Chromosome | Chromosome/Scaffold: 3 Start: 3816759 End: 3818760 |
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 | 26 | 246 | 0 |
GLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHEANNGLDIAIRLLEPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVE PPPEGRLPQATKGVDHLRDVFSRMGLNDKDIVALSGGHTLGRCHKERSGFEGAWTQNPLIFDNSYFKEILSGEKEGLLQLPSDKALLDDPLFRPFVERYA ADEDAFFEDYKEAHLKLSELG |
Full Sequence |
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Protein Sequence Length: 252 Download |
MVNKSYPEVK EEYKKAVQRC KRKLRGLIAE KHCAPIVLRL AWHSAGTFDV KTKTGGPFGT 60 IRHPQELAHE ANNGLDIAIR LLEPIKELFP ILSYADFYQL AGVVAVEITG GPEIPFHPGR 120 LDKVEPPPEG RLPQATKGVD HLRDVFSRMG LNDKDIVALS GGHTLGRCHK ERSGFEGAWT 180 QNPLIFDNSY FKEILSGEKE GLLQLPSDKA LLDDPLFRPF VERYAADEDA FFEDYKEAHL 240 KLSELGFADK E* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 1.0e-66 | 21 | 244 | 252 | + 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 | 2.0e-142 | 7 | 247 | 241 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 1.0e-144 | 2 | 247 | 247 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 1.0e-149 | 6 | 247 | 250 | + 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 | 0 | 1 | 251 | 251 | + 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 | AAF23294.1 | 0 | 1 | 246 | 1 | 246 | AC016661_19 putative ascorbate peroxidase [Arabidopsis thaliana] |
GenBank | ABE65932.1 | 0 | 1 | 251 | 1 | 251 | L-ascorbate peroxidase 1b [Arabidopsis thaliana] |
GenBank | ABK28551.1 | 0 | 1 | 251 | 1 | 251 | unknown [Arabidopsis thaliana] |
EMBL | CAA56340.1 | 0 | 1 | 251 | 1 | 251 | ascorbate peroxidase [Arabidopsis thaliana] |
RefSeq | NP_187575.2 | 0 | 1 | 251 | 1 | 251 | APX2 (ASCORBATE PEROXIDASE 2); L-ascorbate peroxidase [Arabidopsis thaliana] |
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 | 1 | 248 | A Chain A, Crystal Structure Of Nxg1-Deltayniig In Complex With Xllg, A Xyloglucan Derived Oligosaccharide |
PDB | 2xih_A | 0 | 3 | 249 | 1 | 248 | A Chain A, Crystal Structure Of Nxg1-Deltayniig In Complex With Xllg, A Xyloglucan Derived Oligosaccharide |
PDB | 2xif_A | 0 | 3 | 249 | 1 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 3 | 249 | 1 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2ghk_X | 0 | 4 | 249 | 14 | 260 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CK277439 | 249 | 4 | 252 | 0 |
CK261956 | 249 | 4 | 252 | 0 |
CK938554 | 252 | 1 | 252 | 0 |
EX276749 | 249 | 4 | 252 | 0 |
CO363844 | 249 | 4 | 252 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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