IED ID | IndEnz0018001501 |
Enzyme Type ID | peroxidase001501 |
Protein Name |
Versatile peroxidase VPL1 EC 1.11.1.16 Versatile liquid phase peroxidase 1 |
Gene Name | vpl1 |
Organism | Pleurotus eryngii (Boletus of the steppes) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Pleurotaceae Pleurotus Pleurotus eryngii (Boletus of the steppes) |
Enzyme Sequence | MSFKTLSALALALGAAVQFASAAVPLVQKRATCADGRTTANAACCVLFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMSDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS |
Enzyme Length | 361 |
Uniprot Accession Number | Q9UR19 |
Absorption | |
Active Site | ACT_SITE 77; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012"; ACT_SITE 194; /note="Tryptophan radical intermediate"; /evidence="ECO:0000250" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin; Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591, ChEBI:CHEBI:53650; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:9987124}; CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+); Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:9987124}; |
DNA Binding | |
EC Number | 1.11.1.16 |
Enzyme Function | FUNCTION: A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase. {ECO:0000269|PubMed:9987124}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (8); Chain (1); Disulfide bond (4); Glycosylation (1); Helix (18); Metal binding (13); Propeptide (1); Region (1); Signal peptide (1); Site (1); Turn (6) |
Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Lignin degradation;Manganese;Metal-binding;Organic radical;Oxidoreductase;Peroxidase;Secreted;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:9987124}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (7) |
Cross Reference PDB | 4BLK; 4BLL; 4BLN; 4BLX; 4BLY; 4BLZ; 4BM0; |
Mapped Pubmed ID | 24387130; |
Motif | |
Gene Encoded By | |
Mass | 37,596 |
Kinetics | |
Metal Binding | METAL 66; /note=Manganese; /evidence=ECO:0000250; METAL 70; /note=Manganese; /evidence=ECO:0000250; METAL 78; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 90; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 92; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 94; /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 205; /note=Manganese; /evidence=ECO:0000250; METAL 217; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 219; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 222; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 224; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297 |
Rhea ID | RHEA:22396; RHEA:22776 |
Cross Reference Brenda |