y
Basic Information | |
---|---|
Species | Ricinus communis |
Cazyme ID | 29656.m000477 |
Family | AA2 |
Protein Properties | Length: 235 Molecular Weight: 25878.5 Isoelectric Point: 8.2893 |
Chromosome | Chromosome/Scaffold: 29656 Start: 38326 End: 40066 |
Description | ascorbate peroxidase 3 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA2 | 16 | 116 | 5.7e-34 |
LRALISSKSCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEIEYKHEANNGLKIAIDLCEDIKARHPKISYADLYQLAGVVSVEITGGPTIEFVPGRKGK A |
Full Sequence |
---|
Protein Sequence Length: 235 Download |
MDAEYLKEIE KARRDLRALI SSKSCAPIML RLAWHDAGTY DAKTKTGGPN GSIRNEIEYK 60 HEANNGLKIA IDLCEDIKAR HPKISYADLY QLAGVVSVEI TGGPTIEFVP GRKGKAHRER 120 SGFEGAWTKD PLKFDNSYFK KLLGGDSGLL KLPTDKALVE DPIFRQYVER YAGDEDAFFA 180 DYAASHKKLS ELGFTPPARG TLATKCCTLF AQGAVGVALA AALVVLGYYY EAHRN 240 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00314 | plant_peroxidase_like | 7.0e-33 | 10 | 191 | 255 | + 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. | ||
PLN02364 | PLN02364 | 6.0e-67 | 4 | 194 | 237 | + L-ascorbate peroxidase 1 | ||
PLN02879 | PLN02879 | 4.0e-73 | 4 | 194 | 236 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 8.0e-102 | 3 | 197 | 247 | + 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. | ||
PLN02608 | PLN02608 | 1.0e-124 | 2 | 212 | 258 | + L-ascorbate peroxidase |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0004601 | peroxidase activity |
GO:0006979 | response to oxidative stress |
GO:0020037 | heme binding |
GO:0055114 | oxidation-reduction process |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2xj6_A | 0 | 1 | 194 | 7 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xih_A | 0 | 1 | 194 | 7 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xif_A | 0 | 1 | 194 | 7 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 1 | 194 | 7 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2ghk_X | 0 | 1 | 194 | 19 | 258 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |