Detail Information for IndEnz0017000009
IED ID IndEnz0017000009
Enzyme Type ID manganese peroxidase000009
Protein Name Versatile peroxidase VPS1
EC 1.11.1.16
Versatile solid phase peroxidase 1
Gene Name vps1 ps1
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 MAFAKLSAFVLALGATVALGESPTHRCLNKRVTCATGQTTANEACCALFPILDDIQTNLFDGAQCGEEVHESLRLTFHDAIAFSPALTNAGQFGGGGADGSMIIFSDTEPNFHANLGIDEIVEAQKPFIARHNISAADFIQFAGAIGVSNCAGAPRLNFFLGRPDATQIPPDGLVPEPFDDVTKILSRMGDAGFSTVEVVWLLASHTIAAADHVDPSIPGTPFDSTPSTFDSQFFLETMLQGTAFPGTPGNQGEVESPLAGEMRLQSDFLLARDSRSACEWQSMVNNMPKIQNRFTQVMKKLSLLGHNQADLIDCSDVIPVPKTLTKAATFPAGKSQADVEIVCNAAATPFPALASDPGPVTAVPPVPPS
Enzyme Length 370
Uniprot Accession Number Q9UVP6
Absorption
Active Site ACT_SITE 78; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012"; ACT_SITE 201; /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:10187820}; 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:10187820};
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:10187820}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 for manganese oxidation reaction, and around 3 for all the manganese-independent reactions. {ECO:0000269|PubMed:10187820};
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (13); Propeptide (1); Region (1); Signal peptide (1); Site (1)
Keywords 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.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 39,046
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48 uM for manganese {ECO:0000269|PubMed:10187820}; KM=9 uM for H(2)O(2) (in manganese oxidation) {ECO:0000269|PubMed:10187820}; KM=2 uM for H(2)O(2) (in manganese-independent oxidations) {ECO:0000269|PubMed:10187820}; KM=17 uM for methoxyhydroquinone {ECO:0000269|PubMed:10187820}; KM=200 uM for syringol {ECO:0000269|PubMed:10187820}; KM=3500 uM for veratryl alcohol {ECO:0000269|PubMed:10187820}; KM=2 uM for reactive black 5 {ECO:0000269|PubMed:10187820};
Metal Binding METAL 67; /note=Manganese; /evidence=ECO:0000250; METAL 71; /note=Manganese; /evidence=ECO:0000250; METAL 79; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 97; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 99; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 101; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 206; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 207; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 212; /note=Manganese; /evidence=ECO:0000250; METAL 224; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 226; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297; METAL 229; /note=Calcium 2; via carbonyl oxygen; METAL 231; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00297
Rhea ID RHEA:22396; RHEA:22776
Cross Reference Brenda 1.11.1.16;