Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.370590.6 |
Family | AA2 |
Protein Properties | Length: 231 Molecular Weight: 25610.2 Isoelectric Point: 7.128 |
Chromosome | Chromosome/Scaffold: 03678 Start: 282521 End: 287539 |
Description | ascorbate peroxidase 3 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 63 | 230 | 0 |
RALIANRNCAPIMLRLAWHDAGTYDVVTKIGGPNGSIRNEEEFSHGSNNGLKKAIDFCEEVKSKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSN ICPKEGRLPDAKKGAPHLRDIFYRMGLSDKDIVALSGGHTLGRAHPERSGFDGPWTEDPLKFDNSYFV |
Full Sequence |
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Protein Sequence Length: 231 Download |
MSFEGRIIRT IWGSRFFANF ELISLLYESN ALPFGPLYPP PMALPVVDTE YLKEIDKARR 60 DLRALIANRN CAPIMLRLAW HDAGTYDVVT KIGGPNGSIR NEEEFSHGSN NGLKKAIDFC 120 EEVKSKHPKI TYADLYQLAG VVAVEVTGGP TIDFVPGRKD SNICPKEGRL PDAKKGAPHL 180 RDIFYRMGLS DKDIVALSGG HTLGRAHPER SGFDGPWTED PLKFDNSYFV * 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00141 | peroxidase | 3.0e-49 | 58 | 202 | 156 | + Peroxidase. | ||
PLN02364 | PLN02364 | 2.0e-77 | 45 | 229 | 186 | + L-ascorbate peroxidase 1 | ||
PLN02879 | PLN02879 | 3.0e-81 | 43 | 229 | 187 | + L-ascorbate peroxidase | ||
cd00691 | ascorbate_peroxidase | 5.0e-119 | 45 | 230 | 190 | + 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 | 4.0e-154 | 42 | 230 | 189 | + 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 | 42 | 230 | 1 | 189 | ascorbate peroxidase [Gossypium hirsutum] |
GenBank | AAV58827.1 | 0 | 42 | 230 | 1 | 189 | ascorbate peroxidase [Populus tomentosa] |
GenBank | ACT87980.1 | 0 | 42 | 230 | 1 | 189 | ascorbate peroxidase [Jatropha curcas] |
GenBank | ACU24524.1 | 0 | 42 | 230 | 1 | 190 | unknown [Glycine max] |
DDBJ | BAB64351.1 | 0 | 42 | 230 | 1 | 189 | peroxisomal ascorbate peroxidase [Cucurbita cv. Kurokawa Amakuri] |
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 | 45 | 230 | 5 | 191 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_C | 0 | 45 | 230 | 5 | 191 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_B | 0 | 45 | 230 | 5 | 191 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 1apx_A | 0 | 45 | 230 | 5 | 191 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
PDB | 2xj6_A | 0 | 45 | 230 | 5 | 191 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
JG488793 | 231 | 1 | 230 | 0 |
JG535411 | 231 | 1 | 230 | 0 |
JG488258 | 231 | 1 | 230 | 0 |
JG486670 | 231 | 1 | 230 | 0 |
JG487998 | 231 | 1 | 230 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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