y
Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os02g14460.1 |
Family | AA2 |
Protein Properties | Length: 335 Molecular Weight: 35440.4 Isoelectric Point: 7.2629 |
Chromosome | Chromosome/Scaffold: 2 Start: 7959782 End: 7960984 |
Description | Peroxidase superfamily protein |
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 | 60 | 313 | 0 |
IKAERRMGASILRLFFHDCFVQGCDASILLDDVPSKGFVGEKTAGPNTNSIRGYEVIDKIKANVEAACPGVVSCADILALAAREGVNLLGGPSWEVPLGR RDSTTASKSEADSDLPGPSSSLADLVAAFGKKGLAPRDMTALSGAHTIGYAQCQFFRGHIYNDTNVDPLFAAERRRRCPAASGSGDSNLAPLDDMTALAF DNAYYRDLVGRRGLLHSDQELFNGGSQDERVKKYSTDPDLFAGDFVAAMIKMGK |
Full Sequence |
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Protein Sequence Length: 335 Download |
MAAASSTTTR FCLLLALVLP MISSAAAGDD ALPLPMTPSY YRKSCPTLEA IVRGTMLSAI 60 KAERRMGASI LRLFFHDCFV QGCDASILLD DVPSKGFVGE KTAGPNTNSI RGYEVIDKIK 120 ANVEAACPGV VSCADILALA AREGVNLLGG PSWEVPLGRR DSTTASKSEA DSDLPGPSSS 180 LADLVAAFGK KGLAPRDMTA LSGAHTIGYA QCQFFRGHIY NDTNVDPLFA AERRRRCPAA 240 SGSGDSNLAP LDDMTALAFD NAYYRDLVGR RGLLHSDQEL FNGGSQDERV KKYSTDPDLF 300 AGDFVAAMIK MGKICPLTGA AGQIRKNCRV VNSS* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 5.0e-14 | 55 | 311 | 277 | + 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 | 2.0e-32 | 52 | 313 | 291 | + 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 | 8.0e-67 | 52 | 207 | 156 | + Peroxidase. | ||
PLN03030 | PLN03030 | 1.0e-74 | 40 | 332 | 305 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 5.0e-155 | 37 | 331 | 302 | + 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 | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004601 | peroxidase activity |
GO:0005515 | protein binding |
GO:0005576 | extracellular region |
GO:0005618 | cell wall |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAD28869.1 | 0 | 4 | 334 | 2 | 327 | putative bacterial-induced peroxidase precursor [Oryza sativa Japonica Group] |
GenBank | EAY85151.1 | 0 | 10 | 334 | 13 | 335 | hypothetical protein OsI_06506 [Oryza sativa Indica Group] |
GenBank | EEE56633.1 | 0 | 1 | 334 | 1 | 303 | hypothetical protein OsJ_06032 [Oryza sativa Japonica Group] |
RefSeq | NP_001046400.1 | 0 | 4 | 334 | 10 | 335 | Os02g0240100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001046402.1 | 0 | 1 | 334 | 1 | 334 | Os02g0240500 [Oryza sativa (japonica cultivar-group)] |
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 | 1sch_B | 0 | 36 | 332 | 2 | 294 | A Chain A, Peanut Peroxidase |
PDB | 1sch_A | 0 | 36 | 332 | 2 | 294 | A Chain A, Peanut Peroxidase |
PDB | 1qo4_A | 0 | 34 | 334 | 1 | 306 | A Chain A, Peanut Peroxidase |
PDB | 1pa2_A | 0 | 34 | 334 | 1 | 306 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 3atj_B | 0 | 34 | 334 | 1 | 308 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |