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Reviewed, UniProtKB/Swiss-Prot Q8J2V8 (P2OX_TRIMT)

Last modified February 9, 2010. Version 30. 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: p2o
OrganismTricholoma matsutake (Matsutake mushroom) (Tricholoma nauseosum)
Taxonomic identifier40145 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Tricholomataceae › Tricholoma

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Protein attributes

Sequence length564 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose. Acts also on D-xylose, 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. Ref.1

Subunit structure

Homotetramer. Ref.1

Sequence similarities

Belongs to the GMC oxidoreductase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.28 mM for D-glucose

KM=45.8 mM for D-xylose

KM=26.4 mM for L-sorbose

KM=45.0 mM for D-galactose

KM=10.7 mM for 1,5-anhydro-D-glucitol

KM=192 mM for trehalose

KM=329 mM for maltose

KM=295 mM for mannose

KM=174 mM for D-arabinose

Vmax=26.6 µmol/min/mg enzyme with D-glucose as substrate

Vmax=13.4 µmol/min/mg enzyme with D-xylose as substrate

Vmax=17.9 µmol/min/mg enzyme with L-sorbose as substrate

Vmax=5.41 µmol/min/mg enzyme with D-galactose as substrate

Vmax=18.4 µmol/min/mg enzyme with 1,5-anhydro-D-glucitol as substrate

Vmax=14.3 µmol/min/mg enzyme with trehalose as substrate

Vmax=15.1 µmol/min/mg enzyme with maltose as substrate

Vmax=6.02 µmol/min/mg enzyme with mannose as substrate

Vmax=1.87 µmol/min/mg enzyme with D-arabinose as substrate

pH dependence:

Optimum pH is 7.5-8.0. Active from pH 6 to 10. Stable from pH 5 to 11.

Temperature dependence:

Optimum temperature is 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
   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

   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

Propeptide1 – 2525
PRO_0000012358
Chain26 – 564539Pyranose 2-oxidase
PRO_0000012359

Sites

Active site4981 By similarity
Active site5411 By similarity
Binding site3921Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue1581Tele-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict261D → H AA sequence Ref.1
Sequence conflict431A → S AA sequence Ref.1
Sequence conflict4371D → E AA sequence Ref.1
Sequence conflict4781I → M AA sequence Ref.1
Sequence conflict496 – 4972AQ → VL AA sequence Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q8J2V8-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 134790030045FC1B

FASTA56461,942
        10         20         30         40         50         60 
MPIRLSKEKI NDLLQRSQGD LTSSQDEIVH YTDVFIAGSG PIACTYARHI IDNTSTTKVY 

        70         80         90        100        110        120 
MAEIGSQDNP VIGAHHRNSI KFQKDTDKFV NIINGALQPI SISPSDTYQP TLAVAAWAPP 

       130        140        150        160        170        180 
IDPAEGQLVI MGHNPNQEAG LNLPGSAVTR TVGGMATHWT CACPTPHDEE RVNNPVDKQE 

       190        200        210        220        230        240 
FDALLERAKT LLNVHSDQYD DSIRQIVVKE TLQQTLDASR GVTTLPLGVE RRTDNPIYVT 

       250        260        270        280        290        300 
WTGADTVLGD VPKSPRFVLV TETRVTKFIV SETNPTQVVA ALLRNLNTSN DELVVAQSFV 

       310        320        330        340        350        360 
IACGAVCTPQ ILWNSNIRPH ALGRYLSEQS MTFCQIVLKR SIVDSIATDP RFAAKVEAHK 

       370        380        390        400        410        420 
KKHPDDVLPI PFHEPEPQVM IPYTSDFPWH VQVHRYAFGD VGPKADPRVV VDLRFFGKSD 

       430        440        450        460        470        480 
IVEENRVTFG PNPKLRDWEA GVTDTYGMPQ PTFHVKRTNA DGDRDQRMMN DMTNVANILG 

       490        500        510        520        530        540 
GYLPGSYPQF MAPGLAQHIT GTTRIGTDDQ TSVADPTSKV HNFDNLWVGG NGCIPDATAC 

       550        560 
NPTRTSVAYA LKGAEAVVSY LGVS

« Hide

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References

[1]"Purification, characterization, and molecular cloning of a pyranose oxidase from the fruit body of the basidiomycete, Tricholoma matsutake."
Takakura Y., Kuwata S.
Biosci. Biotechnol. Biochem. 67:2598-2607(2003) [PubMed: 14730138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-57 AND 436-502, BIOPHYSICOCHEMICAL PROPERTIES, FAD-BINDING, TETRAMERIZATION.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB043883 mRNA. Translation: BAC24805.1.

3D structure databases

SMRQ8J2V8. Positions 32-559.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14333.
BRENDA1.1.3.10. 276073.

Family and domain databases

InterProIPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
IPR012814. Pyranose_ox.
[Graphical view]
PfamPF05199. GMC_oxred_C. 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_TRIMT
AccessionPrimary (citable) accession number: Q8J2V8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 30 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