| IED ID | IndEnz0007000428 |
| Enzyme Type ID | catalase000428 |
| Protein Name |
Catalase isozyme A CAT-A EC 1.11.1.6 |
| Gene Name | CATA Os02g0115700 LOC_Os02g02400 OJ1442_E05.8-1 OsJ_004973 P0036E06.27-1 |
| 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 | MDPCKFRPSSSFDTKTTTTNAGAPVWNDNEALTVGPRGPILLEDYHLIEKVAHFARERIPERVVHARGASAKGFFECTHDVTDITCADFLRSPGAQTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHHPESLHTFFFLFDDVGIPTDYRHMDGFGVNTYTFVTRDAKARYVKFHWKPTCGVSCLMDDEATLVGGKNHSHATQDLYDSIAAGNFPEWKLFVQVIDPEEEERFDFDPLDDTKTWPEDEVPLRPVGRLVLNRNVDNFFNENEQLAFGPGLVVPGIYYSDDKMLQCRVFAYADTQRYRLGPNYLMLPVNAPKCAHHNNHYDGAMNFMHRDEEVDYYPSRHAPLRHAPPTPITPRPVVGRRQKATIHKQNDFKQPGERYRSWAPDRQERFIRRFAGELAHPKVSPELRAIWVNYLSQCDESLGVKIANRLNVKPSM |
| Enzyme Length | 492 |
| Uniprot Accession Number | Q0E4K1 |
| Absorption | |
| Active Site | ACT_SITE 65; /evidence=ECO:0000255|PROSITE-ProRule:PRU10013; ACT_SITE 138; /evidence=ECO:0000250|UniProtKB:Q9C168 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by beta-mercaptoethanol, sodium azide and potassium cyanide. Slightly repressed by 3-amino-1,2,4-triazole (3-AT). Activity is repressed proportionally to increased concentration of NaCl, KCl and MgCl(2), and, to a lower extent, of LiCl. {ECO:0000269|PubMed:21979082}. |
| Binding Site | BINDING 62; /note=Heme; /evidence=ECO:0000250|UniProtKB:Q9C168; BINDING 102; /note=Heme; /evidence=ECO:0000250|UniProtKB:Q9C168; BINDING 151; /note=Heme; /evidence=ECO:0000250|UniProtKB:Q9C168; BINDING 344; /note=Heme; /evidence=ECO:0000250|UniProtKB:Q9C168; BINDING 355; /note=Heme; /evidence=ECO:0000250|UniProtKB:Q9C168 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:21979082}; |
| DNA Binding | |
| EC Number | 1.11.1.6 |
| Enzyme Function | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity). Involved in environmental stress response. Promotes drought stress tolerance and recovery (Ref.10). {ECO:0000250|UniProtKB:Q55DH8, ECO:0000269|Ref.10}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:21979082}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:21979082}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Compositional bias (1); Erroneous gene model prediction (1); Metal binding (1); Modified residue (1); Region (1); Sequence conflict (1) |
| Keywords | Cell membrane;Cytoplasm;Heme;Hydrogen peroxide;Iron;Membrane;Metal-binding;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Stress response |
| Interact With | |
| Induction | INDUCTION: Abundance in leaves follows a photoperiod-dependent circadian rhythm with an oscillating expression pattern peaking late in the light period (PubMed:21398647, Ref.10). Inhibited by water stress (PubMed:21398647). Repressed by abscisic acid (ABA), drought, high salinity (NaCl) and hydrogen peroxide (H(2)O(2)) treatments (Ref.10). Triggered by zinc oxide nanoparticles (ZnO NPs); this induction is reversed by sodium nitroprusside (SNP, a NO donor) (PubMed:25958266). Accumulates upon infection by the bacterial blight agent X.oryzae pv. Oryzae (Xoo) strain PXO99 (PubMed:27185545). Influenced by heat stress (HS); up-regulated in conditons 35 degrees Celsius day / 27 degrees Celsius night, but repressed in conditions 38 degrees Celsius day / 30 degrees Celsius night (PubMed:29464319). {ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:25958266, ECO:0000269|PubMed:27185545, ECO:0000269|PubMed:29464319, ECO:0000269|Ref.10}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26900141, ECO:0000305|PubMed:21398647}. Cell membrane {ECO:0000269|PubMed:29581216}. |
| Modified Residue | MOD_RES 210; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q10S82 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21631533; 24752476; 25719552; 26197316; 8555444; 8662009; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,698 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 mM for H(2)O(2) (at pH 7.5) {ECO:0000269|PubMed:21979082}; Vmax=0.33 umol/min/g enzyme (at pH 7.5) {ECO:0000269|PubMed:21979082}; Note=kcat is 6.6 min(-1) with H(2)O(2) as substrate (at pH 7.5). {ECO:0000269|PubMed:21979082}; |
| Metal Binding | METAL 348; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:Q9C168 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda |