Detail Information for IndEnz0018000590
IED ID IndEnz0018000590
Enzyme Type ID peroxidase000590
Protein Name Peroxidase 32
Atperox P32
EC 1.11.1.7
ATP16a
PRXR3
Gene Name PER32 P32 At3g32980 T15D2.7 T15D2.9
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MNFSYSSLSTWTTLMTLGCLLLHSSISSAQLTPTFYDNTCPSVFTIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAAPNANSARGFPVIDRMKAAVETACPRTVSCADILTIAAQQAVNLAGGPSWRVPLGRRDSLQAFFALANTNLPAPFFTLPQLKASFQNVGLDRPSDLVALSGGHTFGKNQCQFIMDRLYNFSNTGLPDPTLNTTYLQTLRGQCPRNGNQTVLVDFDLRTPTVFDNKYYVNLKELKGLIQTDQELFSSPNATDTIPLVREYADGTQKFFNAFVEAMNRMGNITPLTGTQGQIRQNCRVVNSNSLLHDVVEIVDFVSSM
Enzyme Length 352
Uniprot Accession Number Q9LHB9
Absorption
Active Site ACT_SITE 71; /note=Proton acceptor
Activity Regulation
Binding Site BINDING 168; /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;
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.; FUNCTION: Exhibits a Ca(2+)-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (5); Metal binding (10); Modified residue (1); Sequence conflict (5); Signal peptide (1); Site (1)
Keywords Calcium;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal;Vacuole
Interact With
Induction INDUCTION: Late induced by infection with an incompatible bacterial plant pathogen. {ECO:0000269|PubMed:11748215}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles.
Modified Residue MOD_RES 30; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"
Post Translational Modification
Signal Peptide SIGNAL 1..29; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12473102; 12566592; 14595688; 15231406; 15539469; 17432890; 18796151; 19228333; 24064926; 28627464;
Motif
Gene Encoded By
Mass 38,847
Kinetics
Metal Binding METAL 72; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 75; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 77; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 79; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 81; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 199; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 200; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 251; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 254; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 259; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297
Rhea ID RHEA:56136
Cross Reference Brenda