Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000234905 |
Family | AA2 |
Protein Properties | Length: 461 Molecular Weight: 51366.2 Isoelectric Point: 6.916 |
Chromosome | Chromosome/Scaffold: 007972473 Start: 26329 End: 31380 |
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 | 162 | 381 | 0 |
YSKNCAPIMLRVAWHDAGTYDARTRNGIPGGPNGSIRNKVELNHSANKGLETAVQICEEVKAKHPKITYADLYQLAGVVAVEITGGPSINFVPGRKDSNQ SPPEGRLPDAKLGASHLREVFYRMGLSDKDIVVLSGGHTLGKANKRSGFEGPWTKEPWKFDNSYFVELLEGQTEGLLQLPTDKALVEDPVFRRYVEXYAK DNDAFFRDYAVSHKKLSELG |
Full Sequence |
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Protein Sequence Length: 461 Download |
MVEFESGELE GGVGEEEEGE LMNHLVLSKA EFSGSLRCNA ILHLRDPPVP ENQRHKKLYE 60 LTWNEVVLGL CELLKGESEG LLKLPADKAL LDDLEFRRDV ELYASLTKKY EQHEKEAKSL 120 SFRIANSVFL LRFYALMAAP IVNKEYLQEI EKARRDLRAL IYSKNCAPIM LRVAWHDAGT 180 YDARTRNGIP GGPNGSIRNK VELNHSANKG LETAVQICEE VKAKHPKITY ADLYQLAGVV 240 AVEITGGPSI NFVPGRKDSN QSPPEGRLPD AKLGASHLRE VFYRMGLSDK DIVVLSGGHT 300 LGKANKRSGF EGPWTKEPWK FDNSYFVELL EGQTEGLLQL PTDKALVEDP VFRRYVEXYA 360 KDNDAFFRDY AVSHKKLSEL GFTQPSXAPK VLVTLTIAAI IAALVLVLLV KTSNLLIDIS 420 IISLKRLSFD GYPATREANR AGLSKGPGSS GRHEKQQREE A |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam00141 | peroxidase | 1.0e-52 | 153 | 362 | 220 | + Peroxidase. |
PLN02364 | PLN02364 | 4.0e-89 | 140 | 382 | 245 | + L-ascorbate peroxidase 1 |
PLN02879 | PLN02879 | 2.0e-91 | 140 | 382 | 244 | + L-ascorbate peroxidase |
cd00691 | ascorbate_peroxidase | 9.0e-137 | 139 | 385 | 256 | + 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 | 7.0e-160 | 137 | 390 | 255 | + 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 | 0.0000002 | 70 | 122 | 188 | 244 | ascorbate peroxidase [Gossypium hirsutum] |
GenBank | AAB52954.1 | 0 | 137 | 393 | 1 | 255 | ascorbate peroxidase [Gossypium hirsutum] |
GenBank | AAD43334.1 | 0 | 137 | 390 | 1 | 252 | AF159254_1 ascorbate peroxidase [Zantedeschia aethiopica] |
GenBank | ACT87980.1 | 0.00002 | 70 | 127 | 188 | 249 | ascorbate peroxidase [Jatropha curcas] |
GenBank | ACT87980.1 | 0 | 137 | 393 | 1 | 255 | ascorbate peroxidase [Jatropha curcas] |
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 | 140 | 384 | 5 | 248 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 2xj6_A | 0.0006 | 70 | 105 | 190 | 225 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 2xih_A | 0 | 140 | 384 | 5 | 248 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 2xih_A | 0.0006 | 70 | 105 | 190 | 225 | B Chain B, Structure Of A Cellulose Synthase - Cellulose Translocation Intermediate |
PDB | 2xif_A | 0 | 140 | 384 | 5 | 248 | A Chain A, The Structure Of Ascorbate Peroxidase Compound Ii |