| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os01g22249.1 |
| Family | AA2 |
| Protein Properties | Length: 348 Molecular Weight: 36180.1 Isoelectric Point: 4.956 |
| Chromosome | Chromosome/Scaffold: 1 Start: 12509592 End: 12519255 |
| Description | Peroxidase superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 42 | 303 | 0 |
| QAVAAAFKNNSGVAAGLIRLHFHDCFVRGCDASVLINGSTTERSAGPNASLRGFEVIDAAKAAVEAACPSTVSCADILAFAARDGIKLTGNVDYQVPAGR RDGNVSIAQDALDNLPPPTATAKELTDKFANKSLTLEDMVVLSGAHTVGRSFCSSFLDRIWNNTTAIVDTGLSPGYAALLRALCPSNANASTPITTAIDV STPATLDNNYYKLLPLDLGLFFSDNQLRVNATMNALVTRFAANETEWKQRFADAMVKMGNIE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 348 Download |
| MAMKCLLVFF LVAFFPGAAV SAGLKVGFYN ETCPSAEALV QQAVAAAFKN NSGVAAGLIR 60 LHFHDCFVRG CDASVLINGS TTERSAGPNA SLRGFEVIDA AKAAVEAACP STVSCADILA 120 FAARDGIKLT GNVDYQVPAG RRDGNVSIAQ DALDNLPPPT ATAKELTDKF ANKSLTLEDM 180 VVLSGAHTVG RSFCSSFLDR IWNNTTAIVD TGLSPGYAAL LRALCPSNAN ASTPITTAID 240 VSTPATLDNN YYKLLPLDLG LFFSDNQLRV NATMNALVTR FAANETEWKQ RFADAMVKMG 300 NIEVLTGGAG QIRLNCNVVN PSSSSSSPVV QLAGEEEAAA AGAVAAS* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00691 | ascorbate_peroxidase | 3.0e-8 | 113 | 299 | 196 | + 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. | ||
| cd00314 | plant_peroxidase_like | 6.0e-22 | 54 | 301 | 279 | + 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. | ||
| pfam00141 | peroxidase | 3.0e-58 | 48 | 189 | 143 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 6.0e-82 | 1 | 316 | 323 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 2.0e-140 | 23 | 316 | 298 | + Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004601 | peroxidase activity |
| GO:0005515 | protein binding |
| GO:0005783 | endoplasmic reticulum |
| GO:0006950 | response to stress |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAH69256.1 | 0 | 1 | 347 | 1 | 347 | TPA: class III peroxidase 13 precursor [Oryza sativa (japonica cultivar-group)] |
| EMBL | CAH69257.1 | 0 | 18 | 316 | 23 | 322 | TPA: class III peroxidase 14 precursor [Oryza sativa (japonica cultivar-group)] |
| GenBank | EAY73798.1 | 0 | 18 | 316 | 23 | 322 | hypothetical protein OsI_01677 [Oryza sativa Indica Group] |
| GenBank | EAZ11685.1 | 0 | 70 | 347 | 103 | 380 | hypothetical protein OsJ_01547 [Oryza sativa Japonica Group] |
| RefSeq | NP_001042905.1 | 0 | 68 | 347 | 1 | 280 | Os01g0326300 [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 | 3hdl_A | 0 | 24 | 320 | 2 | 303 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
| PDB | 1sch_B | 0 | 24 | 320 | 2 | 294 | A Chain A, Peanut Peroxidase |
| PDB | 1sch_A | 0 | 24 | 320 | 2 | 294 | A Chain A, Peanut Peroxidase |
| PDB | 1qo4_A | 0 | 24 | 322 | 3 | 306 | A Chain A, Peanut Peroxidase |
| PDB | 1pa2_A | 0 | 24 | 322 | 3 | 306 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |
