| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT4G37520.1 |
| Family | AA2 |
| Protein Properties | Length: 330 Molecular Weight: 36076.2 Isoelectric Point: 8.78 |
| Chromosome | Chromosome/Scaffold: 4 Start: 17631562 End: 17633249 |
| Description | peroxidase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 38 | 313 | 0 |
| NVEQIVRNAVQKKVQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNNNKAEKDHEENLSLAGDGFDTVIKAKEALDAVPNCRNKVSCADILTMATRDVV NLAGGPQYDVELGRLDGLSSTAASVGGKLPHPTDDVNKLTSLFAKNGLSLNDMIALSGAHTLGFAHCTKVFNRIYTFNKTTKVDPTVNKDYVTELKASCP RNIDPRVAINMDPTTPRQFDNVYYKNLQQGKGLFTSDQVLFTDRRSKPTVDLWANNGQLFNQAFINSMIKLGRVGV | |||
| Full Sequence |
|---|
| Protein Sequence Length: 330 Download |
| MVVVNKTNLL LLLLSLCLTL DLSSAQLRRN FYAGSCPNVE QIVRNAVQKK VQQTFTTIPA 60 TLRLYFHDCF VNGCDASVMI ASTNNNKAEK DHEENLSLAG DGFDTVIKAK EALDAVPNCR 120 NKVSCADILT MATRDVVNLA GGPQYDVELG RLDGLSSTAA SVGGKLPHPT DDVNKLTSLF 180 AKNGLSLNDM IALSGAHTLG FAHCTKVFNR IYTFNKTTKV DPTVNKDYVT ELKASCPRNI 240 DPRVAINMDP TTPRQFDNVY YKNLQQGKGL FTSDQVLFTD RRSKPTVDLW ANNGQLFNQA 300 FINSMIKLGR VGVKTGSNGN IRRDCGAFN* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00141 | peroxidase | 2.0e-5 | 262 | 293 | 32 | + Peroxidase. | ||
| cd00691 | ascorbate_peroxidase | 1.0e-21 | 43 | 314 | 288 | + 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. | ||
| pfam00141 | peroxidase | 1.0e-55 | 43 | 198 | 156 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 1.0e-70 | 28 | 329 | 307 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 2.0e-161 | 26 | 328 | 303 | + 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:0004601 | peroxidase activity |
| GO:0005515 | protein binding |
| GO:0005737 | cytoplasm |
| GO:0006979 | response to oxidative stress |
| GO:0020037 | heme binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAL49862.1 | 0 | 1 | 329 | 1 | 329 | putative peroxidase [Arabidopsis thaliana] |
| GenBank | AAM63630.1 | 0 | 1 | 329 | 1 | 329 | peroxidase, prxr2 [Arabidopsis thaliana] |
| EMBL | CAA67362.1 | 0 | 18 | 329 | 1 | 312 | peroxidase ATP9a [Arabidopsis thaliana] |
| RefSeq | NP_195468.1 | 0 | 1 | 329 | 1 | 329 | peroxidase 50 (PER50) (P50) (PRXR2) [Arabidopsis thaliana] |
| RefSeq | NP_195469.1 | 0 | 1 | 329 | 1 | 329 | peroxidase, putative [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1qo4_A | 0 | 26 | 329 | 2 | 304 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 1pa2_A | 0 | 26 | 329 | 2 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
| PDB | 3hdl_A | 0 | 27 | 329 | 2 | 303 | A Chain A, Crystal Structure Of Highly Glycosylated Peroxidase From Royal Palm Tree |
| PDB | 3atj_B | 0 | 26 | 329 | 2 | 306 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
| PDB | 3atj_A | 0 | 26 | 329 | 2 | 306 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |
