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Reviewed, UniProtKB/Swiss-Prot Q8J136 (P2OX_PENSG)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: poxSG
OrganismPeniophora sp. (strain SG) (White-rot fungus)
Taxonomic identifier204723 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Lachnocladiaceae › Peniophora

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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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 FAD covalently per subunit. Ref.2

Subunit structure

Homotetramer. Ref.2

Subcellular location

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

Sequence similarities

Belongs to the GMC oxidoreductase family.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
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 Potential
Propeptide29 – 3810 By similarity
PRO_0000012346
Chain39 – 623585Pyranose 2-oxidase
PRO_0000012347

Sites

Active site5481
Active site5931
Binding site4481Substrate
Binding site4501Substrate

Amino acid modifications

Modified residue1671Tele-8alpha-FAD histidine

Secondary structure

1 .......................................................................................... 623
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8J136-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4B7DB64A387F43D5

FASTA62369,342
        10         20         30         40         50         60 
MSTSSSDPFF NFAKSSFRSA AAQKASASSL PPLPGPDKKV PGMDIKYDVV IVGSGPIGCT 

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

       130        140        150        160        170        180 
LVVDTLSPTS WQASTFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR 

       190        200        210        220        230        240 
PLLVKDDADA DDAEWDRLYT KAESYFQTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP 

       250        260        270        280        290        300 
LAATRRSPTF VEWSSANTVF DLQNRPNTDA PEERFNLFPA VACERVVRNA LNSEIESLHI 

       310        320        330        340        350        360 
HDLISGDRFE IKADVYVLTA GAVHNTQLLV NSGFGQLGRP NPTNPPELLP SLGSYITEQS 

       370        380        390        400        410        420 
LVFCQTVMST ELIDSVKSDM TIRGTPGELT YSVTYTPGAS TNKHPDWWNE KVKNHMMQHQ 

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

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

       550        560        570        580        590        600 
MEPGLVLHLG GTHRMGFDEK EDNCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS 

       610        620 
LAIKSCEYIK QNFTPSPFTS EAQ

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References

[1]"Pyranose oxidase of the white-rot fungus Peniophora sp. strain SG: Cloning and characterization of the gene, heterologous expression in Escherichia coli, and properties of the recombinant enzyme."
Heckmann-Pohl D.M., Bastian S., Rekowski M.J., Giffhorn F.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp."
Bannwarth M., Bastian S., Heckmann-Pohl D.M., Giffhorn F., Schulz G.E.
Biochemistry 43:11683-11690(2004) [PubMed: 15362852] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), TETRAMERIZATION, COFACTOR, FAD-BINDING SITE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF535193 mRNA. Translation: AAO13382.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TZLX-ray2.35A/B/C/D/E/F/G/H2-623[»]
2F5VX-ray1.41A29-623[»]
2F6CX-ray1.84A29-623[»]
ModBaseSearch...

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_PENSG
AccessionPrimary (citable) accession number: Q8J136
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 42 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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