IED ID | IndEnz0018000639 |
Enzyme Type ID | peroxidase000639 |
Protein Name |
Peroxidase 4 EC 1.11.1.7 |
Gene Name | GSVIVT00023967001 LOC100257005 |
Organism | Vitis vinifera (Grape) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids rosids incertae sedis Vitales Vitaceae Viteae Vitis Vitis vinifera (Grape) |
Enzyme Sequence | MASSSFSIVVVALGVLALFAGSSSAQLSTNFYSKTCPKVFDTVKSGVQSAVSKERRMGASLLRLFFHDCFVNGCDASVLLDDTSSFTGEQTAVPNKNSIRGLNVIDNIKSQVESVCPGVVSCADIIAIAARDSVVILGGPDWDVKLGRRDSKTASLSGANNNIPPPTSSLSNLISKFQAQGLSTRDMVALSGAHTIGQARCTSFRARIYNETNIDSSFAKTRQASCPSASGSGDNNLAPLDLQTPTTFDNYYYKNLINQKGLLHSDQVLYNGGSTDSTVKTYVNNPKTFTSDFVAGMIKMGDITPLTGSEGEIRKSCGKVN |
Enzyme Length | 321 |
Uniprot Accession Number | A7NY33 |
Absorption | |
Active Site | ACT_SITE 67; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:Q42578, 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:Q42578, 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. {ECO:0000305}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (1); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (10); Modified residue (1); Sequence conflict (2); Signal peptide (1); Site (1) |
Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Pyrrolidone carboxylic acid;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516, ECO:0000255|PROSITE-ProRule:PRU00297}. |
Modified Residue | MOD_RES 26; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 34,060 |
Kinetics | |
Metal Binding | METAL 68; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 71; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 73; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 75; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 77; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 194; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 195; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 241; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 244; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297"; METAL 249; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297" |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |