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Protein

Pyranose 2-oxidase

Gene

P2OX

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O2 to H2O2. Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H2O2 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.1 Publication

Catalytic activityi

D-glucose + O2 = 2-dehydro-D-glucose + H2O2.

Cofactori

FAD1 PublicationNote: Binds 1 FAD covalently per subunit.1 Publication

Kineticsi

  1. KM=1.4 mM for D-glucose1 Publication
  2. KM=35.3 mM for 1,5-anhydro-D-glucitol1 Publication

    pH dependencei

    Optimum pH is about 6.5. Active from pH 5 to 9. Stable from pH 3 to 11.1 Publication

    Temperature dependencei

    Optimum temperature is about 50 degrees Celsius. Active from 30 to 65 degrees Celsius. Thermostable for 30 minutes up to 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei448 – 4481SubstrateBy similarity
    Binding sitei450 – 4501SubstrateBy similarity
    Active sitei548 – 5481Proton acceptorBy similarity
    Active sitei593 – 5931By similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyranose 2-oxidase (EC:1.1.3.10)
    Short name:
    P2Ox
    Short name:
    POD
    Short name:
    POx
    Short name:
    PROD
    Short name:
    Pyranose oxidase
    Alternative name(s):
    FAD-oxidoreductase
    Glucose 2-oxidase
    Pyranose:oxygen 2-oxidoreductase
    Gene namesi
    Name:P2OX
    OrganismiTrametes versicolor (White-rot fungus) (Coriolus versicolor)
    Taxonomic identifieri5325 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

    Subcellular locationi

    • Periplasm By similarity

    • Note: Hyphal periplasmic space.By similarity

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi542 – 5421E → K: Increases thermostability up to 65 degrees Celsius and enhances pH stability in alkaline solution. Increases the catalytic efficiency 2-fold for D-glucose and 3-fold for 1,5-anhydro-D-glucitol, mainly by lowering the Km values for these two substrates to 0.74 mM and 14.3 mM, respectively. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727CuratedAdd
    BLAST
    Propeptidei28 – 38111 PublicationPRO_0000012356Add
    BLAST
    Chaini39 – 623585Pyranose 2-oxidasePRO_0000012357Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei167 – 1671Tele-8alpha-FAD histidineBy similarity

    Post-translational modificationi

    Not glycosylated.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP79076.
    SMRiP79076. Positions 43-619.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.50.50.60. 4 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR007867. GMC_OxRtase_C.
    IPR012814. P2OX.
    [Graphical view]
    PfamiPF05199. GMC_oxred_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    TIGRFAMsiTIGR02462. pyranose_ox. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P79076-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTSSSDPFF NFTKSSFRSA AAQKASATSL PPLPGPDKKV PGMDIKYDVV
    60 70 80 90 100
    IVGSGPIGCT YARELVEAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI
    110 120 130 140 150
    DKFVNVIQGQ LMSVSVPVNT LVIDTLSPTS WQASSFFVRN GSNPEQDPLR
    160 170 180 190 200
    NLSGQAVTRV VGGMSTHWTC ATPRFDREQR PLLVKDDQDA DDAEWDRLYT
    210 220 230 240 250
    KAESYFKTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP LAATRRSPTF
    260 270 280 290 300
    VEWSSANTVF DLQNRPNTDA PNERFNLFPA VACERVVRNT SNSEIESLHI
    310 320 330 340 350
    HDLISGDRFE IKADVFVLTA GAVHNAQLLV NSGFGQLGRP DPANPPQLLP
    360 370 380 390 400
    SLGSYITEQS LVFCQTVMST ELIDSVKSDM IIRGNPGDLG YSVTYTPGAE
    410 420 430 440 450
    TNKHPDWWNE KVKNHMMQHQ EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH
    460 470 480 490 500
    RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK EENKLWFSDK ITDTYNMPQP
    510 520 530 540 550
    TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF MEPGLVLHLG
    560 570 580 590 600
    GTHRMGFDEQ EDKCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS
    610 620
    LAIKSCEYIK NNFTPSPFTD QAE
    Length:623
    Mass (Da):69,495
    Last modified:May 1, 1997 - v1
    Checksum:i5D3FC81B35FA5B54
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D73369 mRNA. Translation: BAA11119.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D73369 mRNA. Translation: BAA11119.1.

    3D structure databases

    ProteinModelPortaliP79076.
    SMRiP79076. Positions 43-619.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    Gene3Di3.50.50.60. 4 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR007867. GMC_OxRtase_C.
    IPR012814. P2OX.
    [Graphical view]
    PfamiPF05199. GMC_oxred_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 2 hits.
    TIGRFAMsiTIGR02462. pyranose_ox. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor in Escherichia coli."
      Nishimura I., Okada K., Koyama Y.
      J. Biotechnol. 52:11-20(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-63; 92-98; 186-207; 215-225; 378-411; 491-513 AND 611-621, CHARACTERIZATION, TETRAMERIZATION.
      Strain: ATCC 62976 / IAM 13013 / NBRC 30340 / FES 1030 / Ps-4a.
      Tissue: Mycelium.
    2. "Purification and properties of pyranose oxidase from Coriolus versicolor."
      Machida Y., Nakanishi T.
      Agric. Biol. Chem. 48:2463-2470(1984)
      [AGRICOLA] [Europe PMC]
      Cited for: FAD-BINDING.
    3. "Pyranose oxidase, a major source of H(2)O(2) during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida."
      Daniel G., Volc J., Kubatova E.
      Appl. Environ. Microbiol. 60:2524-2532(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Improvement in thermal stability and reactivity of pyranose oxidase from Coriolus versicolor by random mutagenesis."
      Masuda-Nishimura I., Minamihara T., Koyama Y.
      Biotechnol. Lett. 21:203-207(1999)
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TETRAMERIZATION, MUTAGENESIS OF GLU-542.

    Entry informationi

    Entry nameiP2OX_TRAVE
    AccessioniPrimary (citable) accession number: P79076
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: May 1, 1997
    Last modified: March 16, 2016
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.