| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10025942m |
| Family | AA2 |
| Protein Properties | Length: 282 Molecular Weight: 30921 Isoelectric Point: 8.4377 |
| Chromosome | Chromosome/Scaffold: 1 Start: 1730934 End: 1732706 |
| Description | ascorbate peroxidase 5 |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 22 | 242 | 0 |
| ALISSRNCAPIMLRLAWHDAGTYDAKKKTGGPNGSIRFKDELNRSHNNGLEKAVAFCEEVKAKHPRVSYADLYQLAGVVAVEVTGGPAIQFSPGRKDADS PDEGELPDPNQGASHLRTLFSRMGLSDRDIVALSGGHTLGRAHKDRSDFEGAWTQDPLKFDNSYFVELLKGETPGLLQLKTDKALLGDSKFHPYVELYAK EENVFFKDYANSHKKLSELGF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 282 Download |
| MAVNVDAEYL KEIEKTRRDL RALISSRNCA PIMLRLAWHD AGTYDAKKKT GGPNGSIRFK 60 DELNRSHNNG LEKAVAFCEE VKAKHPRVSY ADLYQLAGVV AVEVTGGPAI QFSPGRKDAD 120 SPDEGELPDP NQGASHLRTL FSRMGLSDRD IVALSGGHTL GRAHKDRSDF EGAWTQDPLK 180 FDNSYFVELL KGETPGLLQL KTDKALLGDS KFHPYVELYA KEENVFFKDY ANSHKKLSEL 240 GFNPPRKIPS AVTQQTLGIA VAAAVVIFTI CYEATRGGGK K* 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 5.0e-57 | 14 | 239 | 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 | 5.0e-98 | 5 | 242 | 240 | + L-ascorbate peroxidase 1 | ||
| PLN02879 | PLN02879 | 3.0e-102 | 5 | 242 | 239 | + L-ascorbate peroxidase | ||
| cd00691 | ascorbate_peroxidase | 8.0e-145 | 2 | 245 | 253 | + 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 | 8.0e-161 | 5 | 276 | 281 | + 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 - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAP72144.1 | 0 | 19 | 278 | 1 | 260 | AF441714_1 putative ascorbate peroxidase APX5 [Arabidopsis thaliana] |
| GenBank | AAS46016.1 | 0 | 1 | 247 | 3 | 250 | peroxisomal ascorbate peroxidase [Vigna unguiculata] |
| DDBJ | BAB64351.1 | 0 | 5 | 244 | 6 | 246 | peroxisomal ascorbate peroxidase [Cucurbita cv. Kurokawa Amakuri] |
| DDBJ | BAG09367.1 | 0 | 1 | 247 | 3 | 250 | peroxisomal ascorbate peroxidase [Glycine max] |
| RefSeq | NP_195321.1 | 0 | 1 | 278 | 1 | 278 | APX5 (ASCORBATE PEROXIDASE 5); L-ascorbate peroxidase/ heme binding / peroxidase [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1apx_D | 0 | 4 | 242 | 6 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 0 | 4 | 242 | 6 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 0 | 4 | 242 | 6 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 0 | 4 | 242 | 6 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 2xj6_A | 0 | 4 | 242 | 6 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
