| IED ID | IndEnz0018000847 |
| Enzyme Type ID | peroxidase000847 |
| Protein Name |
Pyranose 2-oxidase P2Ox POD POx PROD Pyranose oxidase EC 1.1.3.10 FAD-oxidoreductase Glucose 2-oxidase Pyranose:oxygen 2-oxidoreductase |
| Gene Name | P2OX |
| Organism | Trametes versicolor (White-rot fungus) (Coriolus versicolor) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Polyporaceae (bracket fungi) Trametes Trametes versicolor (White-rot fungus) (Coriolus versicolor) |
| Enzyme Sequence | MSTSSSDPFFNFTKSSFRSAAAQKASATSLPPLPGPDKKVPGMDIKYDVVIVGSGPIGCTYARELVEAGYKVAMFDIGEIDSGLKIGAHKKNTVEYQKNIDKFVNVIQGQLMSVSVPVNTLVIDTLSPTSWQASSFFVRNGSNPEQDPLRNLSGQAVTRVVGGMSTHWTCATPRFDREQRPLLVKDDQDADDAEWDRLYTKAESYFKTGTDQFKESIRHNLVLNKLAEEYKGQRDFQQIPLAATRRSPTFVEWSSANTVFDLQNRPNTDAPNERFNLFPAVACERVVRNTSNSEIESLHIHDLISGDRFEIKADVFVLTAGAVHNAQLLVNSGFGQLGRPDPANPPQLLPSLGSYITEQSLVFCQTVMSTELIDSVKSDMIIRGNPGDLGYSVTYTPGAETNKHPDWWNEKVKNHMMQHQEDPLPIPFEDPEPQVTTLFQPSHPWHTQIHRDAFSYGAVQQSIDSRLIVDWRFFGRTEPKEENKLWFSDKITDTYNMPQPTFDFRFPAGRTSKEAEDMMTDMCVMSAKIGGFLPGSLPQFMEPGLVLHLGGTHRMGFDEQEDKCCVNTDSRVFGFKNLFLGGCGNIPTAYGANPTLTAMSLAIKSCEYIKNNFTPSPFTDQAE |
| Enzyme Length | 623 |
| Uniprot Accession Number | P79076 |
| Absorption | |
| Active Site | ACT_SITE 548; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:E4QP00; ACT_SITE 593; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 448; /note=Substrate; /evidence=ECO:0000250; BINDING 450; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-glucose + O2 = 2-dehydro-D-glucose + H2O2; Xref=Rhea:RHEA:10552, ChEBI:CHEBI:4167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16609; EC=1.1.3.10; |
| DNA Binding | |
| EC Number | 1.1.3.10 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus. {ECO:0000269|PubMed:16349330}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 50 degrees Celsius. Active from 30 to 65 degrees Celsius. Thermostable for 30 minutes up to 55 degrees Celsius. {ECO:0000269|Ref.4}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 6.5. Active from pH 5 to 9. Stable from pH 3 to 11. {ECO:0000269|Ref.4}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (2); Chain (1); Modified residue (1); Mutagenesis (1); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;FAD;Flavoprotein;Oxidoreductase;Periplasm;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Hyphal periplasmic space. {ECO:0000250}. |
| Modified Residue | MOD_RES 167; /note=Tele-8alpha-FAD histidine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Not glycosylated. |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000305 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,495 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for D-glucose {ECO:0000269|Ref.4}; KM=35.3 mM for 1,5-anhydro-D-glucitol {ECO:0000269|Ref.4}; |
| Metal Binding | |
| Rhea ID | RHEA:10552 |
| Cross Reference Brenda |