| IED ID | IndEnz0018000561 |
| Enzyme Type ID | peroxidase000561 |
| Protein Name |
Cationic peroxidase SPC4 EC 1.11.1.7 |
| Gene Name | Sb03g046810 |
| Organism | Sorghum bicolor (Sorghum) (Sorghum vulgare) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae PACMAD clade Panicoideae Andropogonodae Andropogoneae Sorghinae Sorghum Sorghum bicolor (Sorghum) (Sorghum vulgare) |
| Enzyme Sequence | MSRAPTLAAAAAVAAVVLICSSSTATAADGNARQPPLAPGLSFDFYKRSCPKAESIVRSFVQDAVRRDVGLAAGLLRLHFHDCFVQGCDASVLLDGSATGPGEQQAPPNLTLRPTAFKAINDIHDRLHKECGGTVVSCSDVLALAARDSVVVSGGPSYKVPLGRRDSASFATQQDVLSGLPPPTAAVPALLAVLSKINLDATDLVALSGGHTIGLGHCTSFEDRLFPRPDPTLNATFAGQLRRTCPAKGTDRRTPLDVRTPNAFDNKYYVNLVNREGLFTSDQDLFSNARTRALVDKFARSQRDFFDQFAFSVVKMGQIKVLTGTQGQIRTNCSARNAAGTTMLPWSVSVVEEAADESLGVF |
| Enzyme Length | 362 |
| Uniprot Accession Number | P84516 |
| Absorption | |
| Active Site | ACT_SITE 81; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P22195, ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012" |
| Activity Regulation | |
| Binding Site | BINDING 111; /note="Indole-3-acetate; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; BINDING 181; /note="Substrate; via carbonyl oxygen"; /evidence="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:16650004}; |
| 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 (By similarity). Has a high preference for hydroxycinnamates as substrates. Substrate preference is ferulic acid > p-coumaric acid > N-acetyl tyrosine methyl ester > N-acetyl-tyrosine > tyrosine > catechol > Gly-Tyr-Gly. May be involved in the formation of diferulate linkages in the plant cell wall (PubMed:16650004). {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:16650004}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loss of activity at temperature above 55 degrees Celsius. In the presence of excess calcium, full activity is kept at 65 degrees Celsius for 90 minutes.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.8 with 2.2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, 5.5 with ferulic acid as substrate, and 6.5 with N-acetyl-L-tyrosine as substrate.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Binding site (2); Chain (1); Disulfide bond (4); Glycosylation (3); Helix (17); Metal binding (11); Signal peptide (1); Site (1); Turn (4) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:16650004}. |
| Modified Residue | |
| Post Translational Modification | PTM: The proportions of glycoforms I and II are 35% and 65% respectively. |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000269|PubMed:16650004 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5AOG; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 38,452 |
| Kinetics | |
| Metal Binding | METAL 82; /note="Calcium 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 85; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 87; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 89; /note="Calcium 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 91; /note="Calcium 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 211; /note="Iron (heme b axial ligand); via tele nitrogen"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 212; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 257; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 260; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 263; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"; METAL 265; /note="Calcium 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG" |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda | 1.11.1.7; |