Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_020_00110.4 |
Family | AA2 |
Protein Properties | Length: 246 Molecular Weight: 26588.2 Isoelectric Point: 4.611 |
Chromosome | Chromosome/Scaffold: 20 Start: 953381 End: 957620 |
Description | ascorbate peroxidase 6 |
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 | 25 | 239 | 0 |
VSKGKAAGLLRLVFHDAGTFDKSDNSGGMNGSIVYELDRPENAGLKKSVKILEKARSELDEREQVSWADMIAVAGAEAVSVCGGPVIPVQLGRVDSMVPD PEGKLPEESLDAFGLKQCFLGKGFSTQELVALSGAHTLGSKGFGNPIAFDNTYFKILLEKPWLSSAGMSNMVGLPSDRALPEDDECLRWIKIYADDQNTF FEDFKNAYIKLVNSG |
Full Sequence |
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Protein Sequence Length: 246 Download |
MSESIDDVNA AVTYQTLQEG IKKVVSKGKA AGLLRLVFHD AGTFDKSDNS GGMNGSIVYE 60 LDRPENAGLK KSVKILEKAR SELDEREQVS WADMIAVAGA EAVSVCGGPV IPVQLGRVDS 120 MVPDPEGKLP EESLDAFGLK QCFLGKGFST QELVALSGAH TLGSKGFGNP IAFDNTYFKI 180 LLEKPWLSSA GMSNMVGLPS DRALPEDDEC LRWIKIYADD QNTFFEDFKN AYIKLVNSGV 240 SWKTI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02879 | PLN02879 | 1.0e-39 | 13 | 243 | 255 | + L-ascorbate peroxidase | ||
pfam00141 | peroxidase | 2.0e-44 | 14 | 220 | 215 | + Peroxidase. | ||
PLN02608 | PLN02608 | 5.0e-45 | 24 | 235 | 224 | + L-ascorbate peroxidase | ||
cd00314 | plant_peroxidase_like | 7.0e-66 | 30 | 237 | 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. | ||
cd00691 | ascorbate_peroxidase | 5.0e-72 | 10 | 242 | 249 | + 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 | ACU18323.1 | 0 | 14 | 245 | 88 | 319 | unknown [Glycine max] |
RefSeq | NP_194958.2 | 0 | 9 | 245 | 93 | 329 | APX6; L-ascorbate peroxidase/ heme binding / peroxidase [Arabidopsis thaliana] |
RefSeq | XP_002282677.1 | 0 | 14 | 245 | 99 | 330 | PREDICTED: similar to APX6 (ASCORBATE PEROXIDASE 6); L-ascorbate peroxidase [Vitis vinifera] |
RefSeq | XP_002309628.1 | 0 | 1 | 245 | 87 | 337 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515511.1 | 0 | 14 | 245 | 97 | 328 | L-ascorbate peroxidase 1, cytosolic, putative [Ricinus communis] |
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 | 4e-37 | 13 | 241 | 3 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xih_A | 4e-37 | 13 | 241 | 3 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xif_A | 4e-37 | 13 | 241 | 3 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 4e-37 | 13 | 241 | 3 | 247 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2ghk_X | 4e-37 | 13 | 241 | 15 | 259 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT758480 | 226 | 21 | 246 | 0 |
DR948231 | 208 | 39 | 246 | 0 |
DW503037 | 231 | 14 | 244 | 0 |
DW502843 | 231 | 14 | 244 | 0 |
DW502844 | 231 | 14 | 244 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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