| IED ID | IndEnz0018000065 |
| Enzyme Type ID | peroxidase000065 |
| Protein Name |
L-ascorbate peroxidase 2, cytosolic EC 1.11.1.11 L-ascorbate peroxidase 1b APX1b AtAPx02 |
| Gene Name | APX2 APX1B At3g09640 F11F8_23 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MVKKSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLDPIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGRMGLNDKDIVALSGGHTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKLSELGFADKE |
| Enzyme Length | 251 |
| Uniprot Accession Number | Q1PER6 |
| Absorption | |
| Active Site | ACT_SITE 43; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| 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; |
| DNA Binding | |
| EC Number | 1.11.1.11 |
| Enzyme Function | FUNCTION: Plays a key role in hydrogen peroxide removal. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Erroneous gene model prediction (1); Metal binding (6); Sequence conflict (3); Site (1) |
| Keywords | Calcium;Cytoplasm;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Potassium;Reference proteome |
| Interact With | |
| Induction | INDUCTION: By excess light treatment, by wounding and by heat-shock stress. {ECO:0000269|PubMed:12068123, ECO:0000269|PubMed:12609042, ECO:0000269|PubMed:15086807, ECO:0000269|PubMed:9144965}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10402422; 10412906; 10837263; 11005203; 11027730; 11158440; 11448761; 11473579; 11483357; 11598218; 11862948; 11997373; 11997377; 12626114; 12685046; 12694594; 12805617; 12949616; 12954611; 14722088; 14749482; 15187287; 15308753; 1558944; 16034597; 16649111; 16897488; 17059409; 17080642; 18055584; 18212028; 19638476; 20639446; 20736450; 20862491; 21441406; 21918379; 22286229; 23073024; 23183257; 23314084; 23918368; 24591719; 24769482; 25783413; 26157451; 27320381; 28603528; 29196259; 29785518; 29877633; 30301775; 30329122; 30635071; 31257201; 32423827; 32987853; 7480322; 8534847; 8539286; 8587977; 8717134; 9290648; 9291097; 9306697; 9625709; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,006 |
| Kinetics | |
| 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 185; /note=Potassium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 187; /note=Potassium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:22996 |
| Cross Reference Brenda |