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Reviewed, UniProtKB/Swiss-Prot P79076 (P2OX_TRAVE)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Pyranose 2-oxidase
      Short name=P2Ox
      Short name=Pyranose oxidase
      Short name=PROD
      Short name=POD
      Short name=POx
    EC=1.1.3.10
Alternative name(s):
    Pyranose:oxygen 2-oxidoreductase
    Glucose 2-oxidase
    FAD-oxidoreductase
Gene names
Name: P2OX
OrganismTrametes versicolor (White-rot fungus) (Coriolus versicolor)
Taxonomic identifier5325 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

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Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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. Ref.3

Catalytic activity

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

Cofactor

Binds 1 FAD covalently per subunit. Ref.2

Subunit structure

Homotetramer. Ref.1 Ref.4

Subcellular location

Periplasm By similarity. Note: Hyphal periplasmic space By similarity.

Post-translational modification

Not glycosylated.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.4 mM for D-glucose

KM=35.3 mM for 1,5-anhydro-D-glucitol

pH dependence:

Optimum pH is about 6.5. Active from pH 5 to 9. Stable from pH 3 to 11.

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.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

pyranose oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Probable
Propeptide28 – 3811
PRO_0000012356
Chain39 – 623585Pyranose 2-oxidase
PRO_0000012357

Sites

Active site5481 By similarity
Active site5931 By similarity
Binding site4481Substrate By similarity
Binding site4501Substrate By similarity

Amino acid modifications

Modified residue1671Tele-8alpha-FAD histidine By similarity

Experimental info

Mutagenesis5421E → 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. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P79076-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 5D3FC81B35FA5B54

FASTA62369,495
        10         20         30         40         50         60 
MSTSSSDPFF NFTKSSFRSA AAQKASATSL PPLPGPDKKV PGMDIKYDVV IVGSGPIGCT 

        70         80         90        100        110        120 
YARELVEAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNT 

       130        140        150        160        170        180 
LVIDTLSPTS WQASSFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR 

       190        200        210        220        230        240 
PLLVKDDQDA DDAEWDRLYT KAESYFKTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP 

       250        260        270        280        290        300 
LAATRRSPTF VEWSSANTVF DLQNRPNTDA PNERFNLFPA VACERVVRNT SNSEIESLHI 

       310        320        330        340        350        360 
HDLISGDRFE IKADVFVLTA GAVHNAQLLV NSGFGQLGRP DPANPPQLLP SLGSYITEQS 

       370        380        390        400        410        420 
LVFCQTVMST ELIDSVKSDM IIRGNPGDLG YSVTYTPGAE TNKHPDWWNE KVKNHMMQHQ 

       430        440        450        460        470        480 
EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK 

       490        500        510        520        530        540 
EENKLWFSDK ITDTYNMPQP TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF 

       550        560        570        580        590        600 
MEPGLVLHLG GTHRMGFDEQ EDKCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS 

       610        620 
LAIKSCEYIK NNFTPSPFTD QAE

« Hide

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References

[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: 9025322] [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 / FES 1030 / IAM 13013 / IFO 30340 / 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: IND85055664]
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: 16349330] [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.

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Cross-references

Sequence databases

D73369 mRNA. Translation: BAA11119.1.

3D structure databases

SMRP79076. Positions 43-619.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.3.10. 276061.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR012814. Pyranose_ox.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR02462. pyranose_ox. 1 hit.
PROSITEPS00623. GMC_OXRED_1. False negative.
PS00624. GMC_OXRED_2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameP2OX_TRAVE
AccessionPrimary (citable) accession number: P79076
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents