| IED ID | IndEnz0007000019 |
| Enzyme Type ID | catalase000019 |
| Protein Name |
Catalase isozyme C CAT-C OsCatC EC 1.11.1.6 Protein NITRIC OXIDE EXCESS 1 |
| Gene Name | CATC CAT1 NOE1 LOC_Os03g03910 Os03g0131200 OsJ_09293 OSNPB_030131200 |
| 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 | MDPYKHRPSSSFNGPLWSTNSGAPVWNNNNSLTVGSRGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDITHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAIKFYTREGNWDLVGNNFPVFFIRDGMKFPDMVHSLKPNPKSHVQENWRILDFFSHHPESLHMFTFLFDDIGIPADYRHMDGSGVNTYTLVNRAGKSHYVKFHWKPTCGVKSLLDDEAVTVGGTNHSHATQDLYDSIAAGNFPEWKLFIQTIDPDHEDRFDFDPLDVTKTWPEDIVPLQPVGRMVLNRNIDNFFSENEQLAFCPGIIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLLLPPNAPKCAHHNNHYDGFMNFMHRDEEVDYFPSRYDPAKHAPRYPIPSATLTGRREKVVIAKENNFKQPGERYRSWDPARQDRFIKRWIDALSDPRLTHEIRSIWLSYWSQADRSLGQKLASRLSAKPSM |
| Enzyme Length | 492 |
| Uniprot Accession Number | Q10S82 |
| 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, LiCl and MgCl(2). {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, ECO:0000269|PubMed:29581216}; |
| 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. Responsible for the redox homeostasis in leaves. Prevents nitric oxide (NO) accumulation and subsequent NO-mediated leaf cell death as well as the S-nitrosylation of specific proteins (e.g. glyceraldehyde 3-phosphate dehydrogenase and thioredoxin) by degrading H(2)O(2) (PubMed:22106097, PubMed:23331502). Involved in photorespiration. Promotes drought stress tolerance and recovery (Ref.13). Involved in NO-mediated enhanced tolerance to zinc oxide nanoparticles (ZnO NPs)-induced phytotoxicity (PubMed:25958266). Participates in melatonin-mediated detoxification (PubMed:25912474). {ECO:0000269|PubMed:22106097, ECO:0000269|PubMed:25912474, ECO:0000269|PubMed:25958266, ECO:0000269|Ref.13, ECO:0000303|PubMed:23331502}. |
| 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 7. {ECO:0000269|PubMed:21979082}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Cross-link (1); Metal binding (1); Modified residue (1); Motif (1); Mutagenesis (3); Sequence conflict (2) |
| Keywords | Cell membrane;Glyoxysome;Heme;Hydrogen peroxide;Iron;Membrane;Metal-binding;Oxidoreductase;Peroxidase;Peroxisome;Phosphoprotein;Reference proteome;Stress response;Thioether bond |
| Interact With | |
| Induction | INDUCTION: Abundance in leaves follows a light-dependent rhythm with an oscillating expression pattern peaking early in the light period (PubMed:21398647, PubMed:23331502). Inhibited by water stress and abscisic acid (ABA) in a concentration-dependent manner (PubMed:21398647, PubMed:23331502). Enhanced by ABA biosynthesis inhibitors nordihydroguaiaretic acid and tungstate under water stress (PubMed:21398647). Slightly affected by high salinity and hydrogen peroxide (H(2)O(2)) treatments (PubMed:23331502). Accumulates upon infection by the bacterial blight agent X.oryzae pv. Oryzae (Xoo) strain PXO99 (PubMed:27185545). Repressed by cadmium (Cd) (PubMed:28969789). {ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:23331502, ECO:0000269|PubMed:27185545, ECO:0000269|PubMed:28969789}. |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:26900141, ECO:0000305|PubMed:21398647}. Glyoxysome {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:29581216}. |
| Modified Residue | MOD_RES 210; /note=Phosphotyrosine; by STRK1; /evidence=ECO:0000269|PubMed:29581216 |
| Post Translational Modification | PTM: Activated by STRK1-mediated phosphorylation at Tyr-210 upon salt and oxidative stress. {ECO:0000269|PubMed:29581216}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 2102847; |
| Motif | MOTIF 484..492; /note=Peroxisome targeting signal; /evidence=ECO:0000305|PubMed:21398647 |
| Gene Encoded By | |
| Mass | 56,764 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43 mM for H(2)O(2) (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:26900141}; KM=40 mM for H(2)O(2) (at pH 7.5) {ECO:0000269|PubMed:21979082}; Vmax=251 mmol/min/mg enzyme (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:26900141}; Vmax=0.03 umol/min/g enzyme (at pH 7.5) {ECO:0000269|PubMed:21979082}; Note=kcat is 0.5 min(-1) with H(2)O(2) as substrate (at pH 7.5) (PubMed:21979082). kcat is 28 sec(-1) with H(2)O(2) as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:26900141). {ECO:0000269|PubMed:21979082, ECO:0000269|PubMed:26900141}; |
| Metal Binding | METAL 348; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:Q9C168 |
| Rhea ID | RHEA:20309 |
| Cross Reference Brenda |