| IED ID | IndEnz0018000055 |
| Enzyme Type ID | peroxidase000055 |
| Protein Name |
L-ascorbate peroxidase 1, cytosolic APXa EC 1.11.1.11 OsAPx1 |
| Gene Name | APX1 Os03g0285700 LOC_Os03g17690 OsJ_009999 OSJNBa0013D02.10 |
| 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 | MAKNYPVVSAEYQEAVEKARQKLRALIAEKSCAPLMLRLAWHSAGTFDVSSKTGGPFGTMKTPAELSHAANAGLDIAVRMLEPIKEEIPTISYADFYQLAGVVAVEVSGGPAVPFHPGREDKPAPPPEGRLPDATKGSDHLRQVFGAQMGLSDQDIVALSGGHTLGRCHKERSGFEGPWTRNPLQFDNSYFTELLSGDKEGLLQLPSDKALLSDPAFRPLVEKYAADEKAFFEDYKEAHLKLSELGFADA |
| Enzyme Length | 250 |
| Uniprot Accession Number | Q10N21 |
| Absorption | |
| Active Site | ACT_SITE 42; /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. {ECO:0000269|PubMed:15685422}. |
| 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); Compositional bias (1); Initiator methionine (1); Metal binding (5); Region (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 hydrogen peroxide in leaves (PubMed:25546583). {ECO:0000269|PubMed:11181723, ECO:0000269|PubMed:12203890, ECO:0000269|PubMed:14644501, ECO:0000269|PubMed:25546583}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14681440}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16287625; 17826739; 17916638; 19472976; 19704658; 20417985; 21489969; 21631533; 22686276; 23257241; 24329817; 24705135; 24748750; 25048895; 25496090; 25719552; 26419216; 26801786; 27095404; 27379617; 29106954; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,156 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 mM for ascorbate {ECO:0000269|PubMed:15685422}; KM=0.3 mM for H(2)O(2) {ECO:0000269|PubMed:15685422}; Vmax=15 mM/min/mg enzyme with ascorbate as substrate {ECO:0000269|PubMed:15685422}; Vmax=1 mM/min/mg enzyme with H(2)O(2) as substrate {ECO:0000269|PubMed:15685422}; |
| Metal Binding | METAL 163; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 164; /note=Potassium; /evidence=ECO:0000250; METAL 180; /note=Potassium; /evidence=ECO:0000250; METAL 182; /note=Potassium; /evidence=ECO:0000250; METAL 187; /note=Potassium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:22996 |
| Cross Reference Brenda | 1.11.1.11; |