Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 899989 |
Family | AA2 |
Protein Properties | Length: 293 Molecular Weight: 32117.3 Isoelectric Point: 5.8881 |
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 | 21 | 246 | 0 |
RELRALIAKKNCAPIMLRLAWHDAGTYDAESKTGGPNGSIRNEAEYSHGANSGLKIALDLCEEVKTKHPKISYADLYQLAGVVAVEVTGGPDISFVPGRK DSNACTDEGRLPDANQGFKHLKDVFYRMGLSDKDIVALSGAHTLGRAHPERSGFDGPWTQDPLKFDNSYFVELLKEEESEGLLKLATDKTLLEVPEFRQY VELYAKDEDAFFRDYAESHKKLSELG |
Full Sequence |
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Protein Sequence Length: 293 Download |
MASATLVVDA DYLKEIDKAR RELRALIAKK NCAPIMLRLA WHDAGTYDAE SKTGGPNGSI 60 RNEAEYSHGA NSGLKIALDL CEEVKTKHPK ISYADLYQLA GVVAVEVTGG PDISFVPGRK 120 DSNACTDEGR LPDANQGFKH LKDVFYRMGL SDKDIVALSG AHTLGRAHPE RSGFDGPWTQ 180 DPLKFDNSYF VELLKEEESE GLLKLATDKT LLEVPEFRQY VELYAKDEDA FFRDYAESHK 240 KLSELGFTTP TSSVTKAITD NSTALAHSAV GVAVAAAVVA FGYFYEIRKR MK* 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 1.0e-49 | 19 | 227 | 219 | + Peroxidase. | ||
PLN02879 | PLN02879 | 2.0e-97 | 8 | 247 | 240 | + L-ascorbate peroxidase | ||
PLN02364 | PLN02364 | 3.0e-100 | 8 | 249 | 243 | + L-ascorbate peroxidase 1 | ||
cd00691 | ascorbate_peroxidase | 5.0e-146 | 7 | 248 | 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. | ||
PLN02608 | PLN02608 | 0 | 3 | 292 | 290 | + 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 | AAB52954.1 | 0 | 7 | 292 | 5 | 288 | ascorbate peroxidase [Gossypium hirsutum] |
GenBank | ABA10744.1 | 0 | 4 | 292 | 2 | 287 | cytosolic ascorbate peroxidase isoform 4 [Solanum lycopersicum] |
EMBL | CAA06823.1 | 0 | 4 | 292 | 2 | 287 | ascorbate peroxidase [Arabidopsis thaliana] |
RefSeq | NP_195226.1 | 0 | 4 | 292 | 2 | 287 | APX3 (ASCORBATE PEROXIDASE 3); L-ascorbate peroxidase [Arabidopsis thaliana] |
RefSeq | XP_002530823.1 | 0 | 7 | 292 | 5 | 288 | 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 | 0 | 7 | 247 | 6 | 246 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 2xih_A | 0 | 7 | 247 | 6 | 246 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 2xif_A | 0 | 7 | 247 | 6 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2xi6_A | 0 | 7 | 247 | 6 | 246 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |
PDB | 2ghk_X | 0 | 7 | 247 | 18 | 258 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |