| IED ID | IndEnz0018000249 |
| Enzyme Type ID | peroxidase000249 |
| Protein Name |
L-ascorbate peroxidase 2, cytosolic EC 1.11.1.11 APXb OsAPx2 |
| Gene Name | APX2 SS622 Os07g0694700 LOC_Os07g49400 OsJ_25704 P0627E10.14 |
| Organism | Oryza sativa subsp. japonica (Rice) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice) |
| Enzyme Sequence | MGSKSYPTVSDEYLAAVGKAKRKLRGLIAEKNCAPLMLRLAWHSAGTFDVSSRTGGPFGTMKNPGEQSHAANAGLDIAVRLLDPIKDQLPILSYADFYQLAGVVAVEVTGGPEVPFHPGRQDKPEPPPEGRLPDATQGSDHLRQVFSAQMGLSDKDIVALSGGHTLGRCHKERSGFEGAWTSNPLIFDNSYFTELVSGEKEGLLQLPSDKALMADPAFRPLVEKYAADEDAFFADYAEAHLKLSELGFAEE |
| Enzyme Length | 251 |
| Uniprot Accession Number | Q9FE01 |
| Absorption | |
| Active Site | ACT_SITE 43; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by p-chloromercuriphenylsulfonic acid (CMPSA). {ECO:0000269|PubMed:15685422}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate; Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11; Evidence={ECO:0000269|PubMed:15685422}; |
| DNA Binding | |
| EC Number | 1.11.1.11 |
| Enzyme Function | FUNCTION: Plays a key role in hydrogen peroxide removal (PubMed:15685422). Plays an important role in plant growth and development by protecting the seedlings from abiotic stresses through scavenging reactive oxygen species. Required for pollen viability (PubMed:23468992). {ECO:0000269|PubMed:15685422, ECO:0000269|PubMed:23468992}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7. {ECO:0000269|PubMed:15685422}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (6); Region (1); Sequence conflict (1); Site (1) |
| Keywords | Calcium;Cytoplasm;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Potassium;Reference proteome;Stress response |
| Interact With | |
| Induction | INDUCTION: By stress and hormones. By infection with rice blast fungus (M.grisea). Circadian-regulation. Expression is higher during the light phase than during the dark phase. Induced by salt stress (PubMed:16397796, PubMed:23468992). Induced by heat shock (PubMed:22196946). Induced by hydrogen peroxide in leaves (PubMed:25546583). Induced by drought and cold stresses (PubMed:23468992). {ECO:0000269|PubMed:14644501, ECO:0000269|PubMed:16397796, ECO:0000269|PubMed:22196946, ECO:0000269|PubMed:23468992, ECO:0000269|PubMed:25546583}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10050312; 10069842; 10095115; 10417331; 10529354; 10625676; 10694063; 10750717; 10792828; 10831839; 11027709; 11181723; 11206976; 11373307; 11432939; 11469581; 11592713; 11696369; 11785954; 11912234; 11971145; 12007664; 12060286; 12092839; 12132582; 12200488; 12223619; 12223840; 12228505; 12232197; 12232279; 12232342; 12428011; 12547196; 14660680; 14672408; 15161194; 15265432; 15292215; 15388961; 15450955; 15509849; 15549232; 15574840; 15587273; 15618434; 15620222; 15655675; 1568478; 15753104; 15803416; 15807780; 15832681; 15890521; 15918879; 15941402; 15980189; 15983871; 16028114; 16093491; 16222091; 16255165; 16275657; 16275672; 16287625; 16457592; 16476162; 16604111; 16623902; 16653141; 16668201; 16668795; 16669062; 16722339; 16981044; 17031545; 17031546; 17088362; 17089164; 17147636; 17209124; 17318583; 17333252; 17350935; 17351248; 17384160; 17406793; 17504087; 17516134; 17541718; 17566055; 17571267; 17586689; 17638114; 17653721; 17657411; 17710555; 17727616; 17826739; 17846498; 17916638; 18029787; 18156215; 18439868; 18644781; 18653690; 18657232; 18759000; 18785901; 18811733; 19038476; 19054337; 19089317; 19123004; 19136647; 19214808; 19248588; 19423186; 19470656; 19680127; 19704658; 19723241; 19887471; 19895414; 19921413; 19969519; 20129631; 20138238; 20144872; 2018495; 20194759; 20213122; 20357140; 20443025; 20463817; 20534332; 20559853; 20569332; 20829342; 20948293; 21038434; 21063744; 21106003; 21172814; 21203887; 21205187; 21251105; 21255162; 21309870; 21338466; 21424536; 21478444; 21491156; 21610725; 21631533; 21756975; 21805151; 21822061; 21883553; 21908855; 21978493; 22139936; 22264357; 22270358; 22289642; 22303248; 22492233; 22522784; 22645600; 22686276; 22722993; 22744984; 22848448; 22891159; 22894565; 22903596; 22990444; 23028019; 23031087; 23070303; 23134977; 23457591; 23509111; 23519921; 23649167; 23717458; 23761487; 23783412; 23831949; 23852542; 23939432; 23957671; 24052265; 24132150; 24192013; 24271621; 24272792; 24286292; 24329817; 24390331; 24401104; 24474809; 24634487; 24682961; 24705135; 24722991; 24743556; 24747952; 24748750; 24787501; 24808099; 24964975; 25036957; 25048895; 25137124; 25195901; 25204204; 25223260; 25429996; 25496090; 25505033; 25634963; 25647327; 25667114; 25725409; 25754405; 25786829; 25807209; 25839778; 25917811; 25951042; 26039478; 26098425; 26102503; 26254327; 26309725; 26419216; 26442027; 26461930; 26479032; 26631184; 26648960; 26662549; 26687010; 26706069; 26801786; 26920613; 26939679; 26941770; 26992055; 27023243; 27149194; 27274069; 27297991; 27359114; 27379617; 27583979; 27684295; 29549445; 2973410; 29907832; 3012110; 7565713; 7724677; 7821431; 8108523; 8278510; 8425060; 9039500; 9107028; 9426607; 9530872; 9744098; 9952435; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,118 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for ascorbate {ECO:0000269|PubMed:15685422}; KM=0.7 mM for H(2)O(2) {ECO:0000269|PubMed:15685422}; Vmax=20 mM/min/mg enzyme with ascorbate as substrate {ECO:0000269|PubMed:15685422}; Vmax=3 mM/min/mg enzyme with H(2)O(2) as substrate {ECO:0000269|PubMed:15685422}; |
| Metal Binding | METAL 164; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 165; /note=Potassium; /evidence=ECO:0000250; METAL 181; /note=Potassium; /evidence=ECO:0000250; METAL 183; /note=Potassium; /evidence=ECO:0000250; METAL 186; /note=Potassium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 188; /note=Potassium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:22996 |
| Cross Reference Brenda | 1.11.1.11; |