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Reviewed, UniProtKB/Swiss-Prot P81156 (GOX_PENAG)

Last modified November 25, 2008. Version 50. 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:
    Glucose oxidase
    EC=1.1.3.4
Alternative name(s):
    Glucose oxyhydrase
      Short name=GOD
    Beta-D-glucose:oxygen 1-oxido-reductase
OrganismPenicillium amagasakiense
Taxonomic identifier63559 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

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Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2).

Cofactor

FAD.

Subunit structure

Homodimer.

Subcellular location

Secreted.

Miscellaneous

This enzyme is widely applied for the determination of glucose in body fluids and in removing residual glucose or oxygen from foods and beverages. Furthermore, glucose oxidase-producing moulds such as aspergillus and penicillium species are used for the biological production of gluconic acid.

Sequence similarities

Belongs to the GMC oxidoreductase family.

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Ontologies

Keywords

   Cellular componentSecreted
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processcellular alcohol metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

glucose 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 – 587587Glucose oxidase
PRO_0000205611

Regions

Nucleotide binding26 – 5530FAD Probable

Sites

Active site5201

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) By similarity
Disulfide bond168 ↔ 210

Secondary structure

1 .............................................................................................. 587
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P81156-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 2827477B3DF4508C

FASTA58763,965
        10         20         30         40         50         60 
YLPAQQIDVQ SSLLSDPSKV AGKTYDYIIA GGGLTGLTVA AKLTENPKIK VLVIEKGFYE 

        70         80         90        100        110        120 
SNDGAIIEDP NAYGQIFGTT VDQNYLTVPL INNRTNNIKA GKGLGGSTLI NGDSWTRPDK 

       130        140        150        160        170        180 
VQIDSWEKVF GMEGWNWDNM FEYMKKAEAA RTPTAAQLAA GHSFNATCHG TNGTVQSGAR 

       190        200        210        220        230        240 
DNGQPWSPIM KALMNTVSAL GVPVQQDFLC GHPRGVSMIM NNLDENQVRV DAARAWLLPN 

       250        260        270        280        290        300 
YQRSNLEILT GQMVGKVLFK QTASGPQAVG VNFGTNKAVN FDVFAKHEVL LAAGSAISPL 

       310        320        330        340        350        360 
ILEYSGIGLK SVLDQANVTQ LLDLPVGINM QDQTTTTVSS RASSAGAGQG QAVFFANFTE 

       370        380        390        400        410        420 
TFGDYAPQAR DLLNTKLDQW AEETVARGGF HNVTALKVQY ENYRNWLLDE DVAFAELFMD 

       430        440        450        460        470        480 
TEGKINFDLW DLIPFTRGSV HILSSDPYLW QFANDPKFFL NEFDLLGQAA ASKLARDLTS 

       490        500        510        520        530        540 
QGAMKEYFAG ETLPGYNLVQ NATLSQWSDY VLQNFRPNWH AVSSCSMMSR ELGGVVDATA 

       550        560        570        580 
KVYGTQGLRV IDGSIPPTQV SSHVMTIFYG MALKVADAIL DDYAKSA

« Hide

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References

[1]"Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases."
Kiess M., Hecht H.-J., Kalisz H.M.
Eur. J. Biochem. 252:90-99(1998) [PubMed: 9523716] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"1.8 and 1.9-A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes."
Wohlfahrt G., Witt S., Hendle J., Schomburg D., Kalisz H.M., Hecht H.-J.
Acta Crystallogr. D 55:969-977(1999) [PubMed: 10216293] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

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Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GPEX-ray1.80A/B1-587[»]
ModBaseSearch...

Family and domain databases

InterProIPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGOX_PENAG
AccessionPrimary (citable) accession number: P81156
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 25, 2008
This is version 50 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