| Basic Information | |
|---|---|
| Species | Phaseolus vulgaris |
| Cazyme ID | Phvul.002G104700.1 |
| Family | AA2 |
| Protein Properties | Length: 301 Molecular Weight: 34380.6 Isoelectric Point: 9.4799 |
| Chromosome | Chromosome/Scaffold: 02 Start: 21073548 End: 21077072 |
| Description | ascorbate peroxidase 3 |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 22 | 252 | 1.6e-34 |
| FITNNKCAPLMLQLAWNDAATGGPNASIRFITKHEAFKDLEKAVEYCEIVKAKLKLKKVSYADLYQLAGVVAIEVTQGPTIDFVPGRKDLNESPRVQIRF LNGEEDARSLRRKFSRMGLSEDKDIVVLCGGHTLTRSMYPKVPMRETPEGETHKDSSKFDERKWTKDPLKFDNSYFKELLSKGASFSRLPIDNALVEDQI FRHYVERYAKDEDIFFKEYAISHKKLSELGF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 301 Download |
| MGEVDEEYLS EIEMARRQLR SFITNNKCAP LMLQLAWNDA ATGGPNASIR FITKHEAFKD 60 LEKAVEYCEI VKAKLKLKKV SYADLYQLAG VVAIEVTQGP TIDFVPGRKD LNESPRVQIR 120 FLNGEEDARS LRRKFSRMGL SEDKDIVVLC GGHTLTRSMY PKVPMRETPE GETHKDSSKF 180 DERKWTKDPL KFDNSYFKEL LSKGASFSRL PIDNALVEDQ IFRHYVERYA KDEDIFFKEY 240 AISHKKLSEL GFDPKKLNQD KGLCQKLNQH KGLVGIGMIS VVLTAILGYL HKKKKNQLKN 300 * |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam00141 | peroxidase | 8.0e-36 | 15 | 232 | 227 | + Peroxidase. |
| PLN02364 | PLN02364 | 5.0e-55 | 4 | 252 | 260 | + L-ascorbate peroxidase 1 |
| PLN02879 | PLN02879 | 7.0e-61 | 3 | 256 | 264 | + L-ascorbate peroxidase |
| cd00691 | ascorbate_peroxidase | 4.0e-88 | 7 | 252 | 262 | + 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 | 5.0e-99 | 4 | 291 | 303 | + 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 | AAL35365.1 | 0 | 4 | 254 | 6 | 246 | AF442387_1 ascorbate peroxidase [Capsicum annuum] |
| GenBank | ABA10744.1 | 0 | 4 | 262 | 6 | 254 | cytosolic ascorbate peroxidase isoform 4 [Solanum lycopersicum] |
| GenBank | ACF06512.1 | 0 | 4 | 256 | 6 | 248 | peroxisome type ascorbate peroxidase [Elaeis guineensis] |
| DDBJ | BAB64351.1 | 0 | 4 | 254 | 6 | 246 | peroxisomal ascorbate peroxidase [Cucurbita cv. Kurokawa Amakuri] |
| RefSeq | NP_001052271.1 | 0 | 4 | 266 | 7 | 259 | Os04g0223300 [Oryza sativa (japonica cultivar-group)] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2cl4_X | 0 | 4 | 252 | 19 | 258 | X Chain X, Ascorbate Peroxidase R172a Mutant |
| PDB | 1apx_D | 0 | 4 | 252 | 7 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_C | 0 | 4 | 252 | 7 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_B | 0 | 4 | 252 | 7 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1apx_A | 0 | 4 | 252 | 7 | 246 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
