| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT3G49110.1 |
| Family | AA2 |
| Protein Properties | Length: 355 Molecular Weight: 38941.3 Isoelectric Point: 6.8629 |
| Chromosome | Chromosome/Scaffold: 3 Start: 18200664 End: 18203142 |
| Description | peroxidase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 45 | 317 | 0 |
| VTNIVRDTIVNELRSDPRIAGSILRLHFHDCFVNGCDASILLDNTTSFRTEKDALGNANSARGFPVIDRMKAAVERACPRTVSCADMLTIAAQQSVTLAG GPSWKVPLGRRDSLQAFLDLANANLPAPFFTLPQLKANFKNVGLDRPSDLVALSGAHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNG NQSVLVDFDLRTPLVFDNKYYVNLKEQKGLIQSDQELFSSPNATDTIPLVRAYADGTQTFFNAFVEAMNRMGN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 355 Download |
| MQFSSSSITS FTWTVLITVG CLMLCASFSD AQLTPTFYDT SCPTVTNIVR DTIVNELRSD 60 PRIAGSILRL HFHDCFVNGC DASILLDNTT SFRTEKDALG NANSARGFPV IDRMKAAVER 120 ACPRTVSCAD MLTIAAQQSV TLAGGPSWKV PLGRRDSLQA FLDLANANLP APFFTLPQLK 180 ANFKNVGLDR PSDLVALSGA HTFGKNQCRF IMDRLYNFSN TGLPDPTLNT TYLQTLRGQC 240 PRNGNQSVLV DFDLRTPLVF DNKYYVNLKE QKGLIQSDQE LFSSPNATDT IPLVRAYADG 300 TQTFFNAFVE AMNRMGNITP TTGTQGQIRL NCRVVNSNSL LHDVVDIVDF VSSM* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00314 | plant_peroxidase_like | 2.0e-36 | 49 | 317 | 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 | 2.0e-63 | 49 | 202 | 154 | + Peroxidase. | ||
| PLN03030 | PLN03030 | 9.0e-74 | 14 | 336 | 330 | + cationic peroxidase; Provisional | ||
| cd00693 | secretory_peroxidase | 3.0e-164 | 32 | 335 | 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:0005773 | vacuole |
| GO:0006800 | oxygen and reactive oxygen species metabolic process |
| GO:0006979 | response to oxidative stress |
| GO:0009416 | response to light stimulus |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAA50677.1 | 0 | 13 | 354 | 12 | 353 | peroxidase [Arabidopsis thaliana] |
| RefSeq | NP_190480.1 | 0 | 1 | 354 | 1 | 354 | PRXCA (PEROXIDASE CA); peroxidase [Arabidopsis thaliana] |
| RefSeq | NP_190481.1 | 0 | 13 | 354 | 12 | 353 | PRXCB (PEROXIDASE CB); peroxidase [Arabidopsis thaliana] |
| RefSeq | NP_850652.1 | 0 | 1 | 354 | 1 | 352 | peroxidase 32 (PER32) (P32) (PRXR3) [Arabidopsis thaliana] |
| Swiss-Prot | P15232 | 0 | 5 | 354 | 3 | 351 | PER1B_ARMRU RecName: Full=Peroxidase C1B; 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 | 32 | 354 | 1 | 323 | A Chain A, Crystal Structure Of Human Clk1 In Complex With 10z-Hymenialdisine |
| PDB | 1w4w_A | 0 | 32 | 354 | 1 | 323 | A Chain A, Ferric Horseradish Peroxidase C1a In Complex With Formate |
| PDB | 7atj_A | 0 | 32 | 339 | 1 | 308 | A Chain A, Ferric Horseradish Peroxidase C1a In Complex With Formate |
| PDB | 6atj_A | 0 | 32 | 339 | 1 | 308 | A Chain A, Recombinant Horseradish Peroxidase C Complex With Ferulic Acid |
| PDB | 1h5m_A | 0 | 32 | 339 | 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 |
