| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT4G36430.1 |
| Family | AA2 |
| Protein Properties | Length: 332 Molecular Weight: 36164 Isoelectric Point: 8.4819 |
| Chromosome | Chromosome/Scaffold: 4 Start: 17204478 End: 17205966 |
| Description | peroxidase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 45 | 312 | 0 |
| IVRSVVAKAVARETRMAASLLRLHFHDCFVQGCDGSLLLDSSGRVATEKNSNPNSKSARGFDVVDQIKAELEKQCPGTVSCADVLTLAARDSSVLTGGPS WVVPLGRRDSRSASLSQSNNNIPAPNNTFQTILSKFNRQGLDITDLVALSGSHTIGFSRCTSFRQRLYNQSGNGSPDMTLEQSFAANLRQRCPKSGGDQI LSVLDIISAASFDNSYFKNLIENKGLLNSDQVLFSSNEKSRELVKKYAEDQGEFFEQFAESMIKMGNI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 332 Download |
| MARLTSFLLL LSLICFVPLC LCDKSYGGKL FPGYYAHSCP QVNEIVRSVV AKAVARETRM 60 AASLLRLHFH DCFVQGCDGS LLLDSSGRVA TEKNSNPNSK SARGFDVVDQ IKAELEKQCP 120 GTVSCADVLT LAARDSSVLT GGPSWVVPLG RRDSRSASLS QSNNNIPAPN NTFQTILSKF 180 NRQGLDITDL VALSGSHTIG FSRCTSFRQR LYNQSGNGSP DMTLEQSFAA NLRQRCPKSG 240 GDQILSVLDI ISAASFDNSY FKNLIENKGL LNSDQVLFSS NEKSRELVKK YAEDQGEFFE 300 QFAESMIKMG NISPLTGSSG EIRKNCRKIN S* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00141 | peroxidase | 0.0002 | 262 | 294 | 33 | + Peroxidase. | ||
| cd00314 | plant_peroxidase_like | 8.0e-31 | 44 | 311 | 298 | + 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 | 1.0e-67 | 46 | 199 | 154 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 4.0e-86 | 33 | 330 | 304 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 2.0e-178 | 29 | 329 | 301 | + 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:0005618 | cell wall |
| GO:0006979 | response to oxidative stress |
| GO:0020037 | heme binding |
| GO:0051707 | response to other organism |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAM61616.1 | 0 | 1 | 331 | 1 | 337 | putative peroxidase [Arabidopsis thaliana] |
| GenBank | ABZ80408.1 | 0 | 1 | 330 | 1 | 330 | class III peroxidase [Casuarina glauca] |
| RefSeq | NP_179406.1 | 0 | 1 | 330 | 1 | 335 | peroxidase, putative [Arabidopsis thaliana] |
| RefSeq | NP_179407.1 | 0 | 1 | 331 | 1 | 337 | peroxidase, putative [Arabidopsis thaliana] |
| RefSeq | NP_195361.1 | 0 | 1 | 331 | 1 | 331 | 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 | 34 | 330 | 7 | 304 | A Chain A, Crystal Structure Of Human Glcat-P Apo Form |
| PDB | 1pa2_A | 0 | 34 | 330 | 7 | 304 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
| PDB | 1qgj_B | 0 | 29 | 331 | 1 | 300 | A Chain A, Arabidopsis Thaliana Peroxidase N |
| PDB | 1qgj_A | 0 | 29 | 331 | 1 | 300 | A Chain A, Arabidopsis Thaliana Peroxidase N |
| PDB | 4a5g_B | 0 | 27 | 330 | 1 | 305 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |
