| IED ID | IndEnz0018000013 |
| Enzyme Type ID | peroxidase000013 |
| Protein Name |
Peroxidase N1 EC 1.11.1.7 Peroxidase B2 Peroxidase B3 |
| Gene Name | poxN1 |
| Organism | Nicotiana tabacum (Common tobacco) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Nicotianoideae Nicotianeae Nicotiana Nicotiana tabacum (Common tobacco) |
| Enzyme Sequence | MEYYHHSINKMAMFMVILVLAIDVTMVLGQGTRVGFYSSTCPRAESIVQSTVRAHFQSDPTVAPGILRMHFHDCFVLGCDGSILIEGSDAERTAIPNRNLKGFDVIEDAKTQIEAICPGVVSCADILALAARDSVVATRGLTWSVPTGRRDGRVSRAADAGDLPAFFDSVDIQKRKFLTKGLNTQDLVALTGAHTIGTAGCAVIRDRLFNFNSTGGPDPSIDATFLPQLRALCPQNGDASRRVGLDTGSVNNFDTSYFSNLRNGRGVLESDQKLWTDASTQVFVQRFLGIRGLLGLTFGVEFGRSMVKMSNIEVKTGTNGEIRKVCSAIN |
| Enzyme Length | 330 |
| Uniprot Accession Number | Q9XIV8 |
| Absorption | |
| Active Site | ACT_SITE 72; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | BINDING 164; /note="Substrate; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000269|PubMed:10364388}; |
| DNA Binding | |
| EC Number | 1.11.1.7 |
| Enzyme Function | FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. Can use NADH, NADPH and monolignols as substrates. {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:10364388, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.7. {ECO:0000269|PubMed:10364388}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (9); Modified residue (1); Natural variant (4); Sequence conflict (13); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Induced rapidly in leaves after wounding, mRNA is detectable 30 minutes after wounding, reaches maximum levels after 4 hours, and decreases slightly after 8 hours. When lower leaves are wounded, mRNA also accumulates in upper, unwounded, leaves. Wound-induced expression is enhanced by spermine, and suppressed by methyl jasmonite and coronatine. Salicylic acid and ethephon have no effect on wound-induced expression. Induced by infection with TMV. {ECO:0000269|PubMed:10795310}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516, ECO:0000255|PROSITE-ProRule:PRU00297}. |
| Modified Residue | MOD_RES 30; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000269|PubMed:10364388 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,732 |
| Kinetics | |
| Metal Binding | METAL 73; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 76; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 78; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 80; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 82; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 194; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 195; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 246; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 254; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297" |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |