y
Basic Information | |
---|---|
Species | Arabidopsis thaliana |
Cazyme ID | AT3G49120.1 |
Family | AA2 |
Protein Properties | Length: 354 Molecular Weight: 38832.1 Isoelectric Point: 7.6968 |
Chromosome | Chromosome/Scaffold: 3 Start: 18207651 End: 18210132 |
Description | peroxidase precursor, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA2 | 43 | 316 | 0 |
NVTNIVRETIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVERACPRTVSCADMLTIAAQQSVTLA GGPSWRVPLGRRDSLQAFLELANANLPAPFFTLPQLKASFRNVGLDRPSDLVALSGGHTFGKNQCQFILDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLN GNRSALVDFDLRTPTVFDNKYYVNLKERKGLIQSDQELFSSPNATDTIPLVRAYADGTQTFFNAFVEAMNRMGN |
Full Sequence |
---|
Protein Sequence Length: 354 Download |
MHFSSSSTSS TWTILITLGC LMLHASLSAA QLTPTFYDRS CPNVTNIVRE TIVNELRSDP 60 RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVERA 120 CPRTVSCADM LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LELANANLPA PFFTLPQLKA 180 SFRNVGLDRP SDLVALSGGH TFGKNQCQFI LDRLYNFSNT GLPDPTLNTT YLQTLRGLCP 240 LNGNRSALVD FDLRTPTVFD NKYYVNLKER KGLIQSDQEL FSSPNATDTI PLVRAYADGT 300 QTFFNAFVEA MNRMGNITPT TGTQGQIRLN CRVVNSNSLL HDVVDIVDFV SSM* 360 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00691 | ascorbate_peroxidase | 4.0e-14 | 54 | 310 | 283 | + 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 | 8.0e-33 | 48 | 316 | 299 | + 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 | 9.0e-63 | 48 | 201 | 154 | + Peroxidase. | ||
PLN03030 | PLN03030 | 2.0e-77 | 13 | 335 | 330 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 6.0e-165 | 31 | 334 | 304 | + 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:0005773 | vacuole |
GO:0005886 | plasma membrane |
GO:0006800 | oxygen and reactive oxygen species metabolic process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAA33377.1 | 0 | 1 | 353 | 1 | 353 | HRPC1 [Armoracia rusticana] |
EMBL | CAA50677.1 | 0 | 1 | 353 | 1 | 353 | peroxidase [Arabidopsis thaliana] |
RefSeq | NP_190480.1 | 0 | 12 | 353 | 13 | 354 | PRXCA (PEROXIDASE CA); peroxidase [Arabidopsis thaliana] |
RefSeq | NP_190481.1 | 0 | 1 | 353 | 1 | 353 | PRXCB (PEROXIDASE CB); peroxidase [Arabidopsis thaliana] |
Swiss-Prot | P00433 | 0 | 1 | 353 | 1 | 353 | PER1A_ARMRU RecName: Full=Peroxidase C1A; Flags: Precursor |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1w4y_A | 0 | 31 | 353 | 1 | 323 | A Chain A, The Structure Of A Protein In Glycosyl Transferase Family 8 From Anaerococcus Prevotii. |
PDB | 1w4w_A | 0 | 31 | 353 | 1 | 323 | A Chain A, Ferric Horseradish Peroxidase C1a In Complex With Formate |
PDB | 7atj_A | 0 | 31 | 338 | 1 | 308 | A Chain A, Ferric Horseradish Peroxidase C1a In Complex With Formate |
PDB | 6atj_A | 0 | 31 | 338 | 1 | 308 | A Chain A, Recombinant Horseradish Peroxidase C Complex With Ferulic Acid |
PDB | 1h5m_A | 0 | 31 | 338 | 1 | 308 | A Chain A, Recombinant Horseradish Peroxidase C Complex With Ferulic Acid |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
betanidin degradation | RXN-8635 | EC-1.11.1.7 | peroxidase |