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Reviewed, UniProtKB/Swiss-Prot Q75ZP8 (P2OX_LYOSH)

Last modified June 16, 2009. Version 22. 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
Synonyms: lsp2o
OrganismLyophyllum shimeji (Hon-shimeji)
Taxonomic identifier47721 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Tricholomataceae › Lyophyllum

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Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 FAD covalently per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the GMC oxidoreductase family.

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Ontologies

Keywords
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Chain1 – 618618Pyranose 2-oxidase
PRO_0000205613

Sites

Active site5401 By similarity
Active site5831 By similarity
Binding site4411Substrate By similarity
Binding site4431Substrate By similarity

Amino acid modifications

Modified residue1701Tele-8alpha-FAD histidine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q75ZP8-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 255B99DF266BC541

FASTA61868,488
        10         20         30         40         50         60 
MSLSTEQMLR DYPRSMQING QIPKNAIHET YGNDGVDVFI AGSGPIGATY AKLCVEAGLR 

        70         80         90        100        110        120 
VVMVEIGAAD SFYAVNAEEG TAVPYVPGYH KKNEIEFQKD IDRFVNVIKG ALQQVSVPVR 

       130        140        150        160        170        180 
NQNVPTLDPG AWSAPPGSSA ISNGKNPHQR EFENLSAEAV TRGVGGMSTH WTCSTPRIHP 

       190        200        210        220        230        240 
PMESLPGIGR PKLSNDPAED DKEWNELYSE AERLIGTSTK EFDESIRHTL VLRSLQDAYK 

       250        260        270        280        290        300 
DRQRIFRPLP LACHRLKNAP EYVEWHSAEN LFHSIYNDDK QKKLFTLLTN HRCTRLALTG 

       310        320        330        340        350        360 
GYEKKIGAAE VRNLLATRNP SSQLDSYIMA KVYVLASGAI GNPQILYNSG FSGLQVTPRN 

       370        380        390        400        410        420 
DSLIPNLGRY ITEQPMAFCQ IVLRQEFVDS VRDDPYGLPW WKEAVAQHIA KNPTDALPIP 

       430        440        450        460        470        480 
FRDPEPQVTT PFTEEHPWHT QIHRDAFSYG AVGPEVDSRV IVDLRWFGAT DPEANNLLVF 

       490        500        510        520        530        540 
QNDVQDGYSM PQPTFRYRPS TASNVRARKM MADMCEVASN LGGYLPTSPP QFMDPGLALH 

       550        560        570        580        590        600 
LAGTTRIGFD KATTVADNNS LVWDFANLYV AGNGTIRTGF GENPTLTSMC HAIKSARSII 

       610 
NTLKGGTDGK NTGEHRNL

« Hide

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References

[1]"Identification and cloning of a novel pyranose oxidase with high catalytic activity from Lyophyllum shimeji and its expression in Escherichia coli."
Takakura Y., Tsutsumi F., Inoue Y., Kuwata S.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

AB119106 mRNA. Translation: BAD12079.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.3.10. 309961.

Family and domain databases

InterProIPR000172. GMC_OxRdtase_N.
IPR012814. Pyranose_ox.
[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_LYOSH
AccessionPrimary (citable) accession number: Q75ZP8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 22 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