| IED ID | IndEnz0018000975 |
| Enzyme Type ID | peroxidase000975 |
| Protein Name |
Catalase isozyme B CAT-B EC 1.11.1.6 |
| Gene Name | CATB Os06g0727200 LOC_Os06g51150 OsJ_021830 P0017G10.17 |
| 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 | MDPYKHRPSSGSNSTFWTTNSGAPVWNNNSALTVGERGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPSPKTNMQENWRIVDFFSHHPESLHMFSFLFDDVGIPLNYRHMEGFGVNTYTLINKDGKPHLVKFHWKPTCGVKCLLDDEAVTVGGTCHSHATKDLTDSIAAGNYPEWKLYIQTIDPDHEDRFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNIDNFFAENEQLAFCPAIIVPGIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAYHNNHHDGSMNFMHRDEEVNYFPSRFDAARHAEKVPIPPRVLTGCREKCVIDKENNFQQAGERYRSFDPARQDRFLQRWVDALSDPRITHELRGIWISYWSQCDASLGQKLASRLNLKPNM |
| Enzyme Length | 492 |
| Uniprot Accession Number | Q0D9C4 |
| 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}; |
| 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). May prevent the excessive accumulation of H(2)O(2) during water stress in response to the accumulation of abscisic acid (ABA) (PubMed:21398647). Involved in the modulation of ROS levels related to root growth regulation (Ref.11). Required for pollen viability and floret fertility upon heat stress (HS) by detoxifying reactive oxygen species (ROS) and malondialdehyde (MDA) accumulation in developing anthers exposed to HS (PubMed:29464319). {ECO:0000250|UniProtKB:Q55DH8, ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:29464319, ECO:0000269|Ref.11}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:21979082}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {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); Region (1); Sequence conflict (4) |
| 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 roots follows a diurnal oscillating expression pattern peaking during the night period (Ref.11). Induced by water stress and abscisic acid (ABA) in a concentration-dependent manner (PubMed:21398647, Ref.11). Activated by salicylic acid (SA) (PubMed:29464319). Repressed by ABA biosynthesis inhibitors nordihydroguaiaretic acid and tungstate under water stress (PubMed:21398647). Induced by high salinity (NaCl) and hydrogen peroxide (H(2)O(2)) treatments (Ref.11). Triggered by zinc oxide nanoparticles (ZnO NPs); this induction is reversed by sodium nitroprusside (SNP, a NO donor) (PubMed:25958266). Repressed by cadmium (Cd) (PubMed:28969789). Inhibited by heat stress (HS) (e.g. 35 degrees Celsius day/27 degrees Celsius night, 38 degrees Celsius day/30 degrees Celsius night) (PubMed:29464319). {ECO:0000269|PubMed:21398647, ECO:0000269|PubMed:25958266, ECO:0000269|PubMed:28969789, ECO:0000269|PubMed:29464319, ECO:0000269|Ref.11}. |
| 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; /evidence=ECO:0000250|UniProtKB:Q10S82 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12223699; 15051048; 16753273; 17506334; 17846498; 21631533; 22672582; 25719552; 8662009; |
| Motif | MOTIF 484..492; /note=Peroxisome targeting signal; /evidence=ECO:0000305|PubMed:21398647 |
| Gene Encoded By | |
| Mass | 56,587 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=66.7 mM for H(2)O(2) (at pH 7.5) {ECO:0000269|PubMed:21979082}; Vmax=1 umol/min/g enzyme (at pH 7.5) {ECO:0000269|PubMed:21979082}; Note=kcat is 20 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 | 1.11.1.6; |