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Reviewed, UniProtKB/Swiss-Prot P59097 (P2OX_TRAHI)

Last modified June 16, 2009. Version 36. 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 hirsuta (White-rot fungus) (Coriolus hirsutus)
Taxonomic identifier5327 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

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Protein attributes

Sequence length622 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, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. 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.

Catalytic activity

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

Cofactor

Binds 1 FAD covalently per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

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

Sequence similarities

Belongs to the GMC oxidoreductase family.

biophysicochemical properties

pH dependence:

Optimum pH is 6. Active and stable from pH 3 to 9.

Temperature dependence:

Optimum temperature is 30-50 degrees Celsius. Active and 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 – 2828 By similarity
Propeptide29 – 379 Ref.1
PRO_0000012352
Chain38 – 622585Pyranose 2-oxidase
PRO_0000012353

Sites

Active site5461 By similarity
Active site5911 By similarity
Binding site4491Substrate By similarity
Binding site4511Substrate By similarity

Amino acid modifications

Modified residue1671Tele-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict601T → S AA sequence Ref.1
Sequence conflict243 – 2442AT → FS AA sequence Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P59097-1 [UniParc].

Last modified November 15, 2002. Version 1.
Checksum: 0B616C02014E7C5B

FASTA62269,082
        10         20         30         40         50         60 
MSASSSDPFH SFAKTSFTSK AAKRATAHSL PPLPGPGDLP PGMNVEYDVA IVGSGPIGCT 

        70         80         90        100        110        120 
YARELVEAGF NVAMFEIGEI DSGLKIGSHK KNTVEYQKNI DKFVNVIQGQ LMPVSVPVNT 

       130        140        150        160        170        180 
MVVDTLSPAS WQASTFFVRN GANPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFEKLQR 

       190        200        210        220        230        240 
PLLVKNDSKA DDAEWDRLYK KAESYFKTGT TQFAESIRHN LVLKKLQEEY KGVRDFQQIP 

       250        260        270        280        290        300 
LAATRQSPTF VEWSSAHTVF DLENRPNKDA PKQRFNLFPA VACTNVRRDN ANSEIVGLDV 

       310        320        330        340        350        360 
RDLHGGKSIT IKAKVYILTA GAVHNAQLLA ASGFGQLGRP DPAKPLPSLL PYLGTHITEQ 

       370        380        390        400        410        420 
TLVFCQTVMS TELINSVTAD MTIVGKPGHP DYSVTYTPGN PNNKHPDWWN EKVKKHMMDH 

       430        440        450        460        470        480 
QEDPLPIPFE DPEPQVTTLF QATHPWHTQI HRDAFSYGAV QQSIDSRLIV DWRFFGRTEP 

       490        500        510        520        530        540 
KEENKLWFSD KITDAYNLRQ PTFDFRFPGG REAEDMMTDM CVMSAKIGGF LPGSYPQFME 

       550        560        570        580        590        600 
PGLVLHLGGT HRMGFDEKAD KCCVDTDSRV FGFKNLFLGG CGNIPTAYAA NPTLTAMSLA 

       610        620 
IKSCEYIKKN FEPSPNPVKH HN

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References

[1]"Nucleic acids encoding polypeptides having pyranose oxidase activity."
Christensen S., Lassen S.F., Schneider P.
Patent number US6146865, 14-NOV-2000
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-62; 232-254; 405-412; 486-491 AND 575-596, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DSM 2987.

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Cross-references

3D structure databases

SMRP59097. Positions 43-615.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.3.10. 119234.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR012814. Pyranose_ox.
[Graphical view]
PfamPF01266. DAO. 1 hit.
PF00732. GMC_oxred_N. 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_TRAHI
AccessionPrimary (citable) accession number: P59097
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: June 16, 2009
This is version 36 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