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P13006 (GOX_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glucose oxidase
EC=1.1.3.4
Alternative name(s):
Beta-D-glucose:oxygen 1-oxido-reductase
Glucose oxyhydrase
Short name=GOD
Gene names
Name:gox
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2.

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 molds such as aspergillus and penicillium species are used for the biological production of gluconic acid.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processalcohol metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncholine dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

glucose oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222Or 48
Chain23 – 605583Glucose oxidase
PRO_0000012338

Regions

Nucleotide binding43 – 7230FAD Probable

Sites

Active site5381 By similarity

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...)
Disulfide bond186 ↔ 228

Secondary structure

1 ...................................................................................................... 605
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13006 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 25243E5ED1D2773B

FASTA60565,638
        10         20         30         40         50         60 
MQTLLVSSLV VSLAAALPHY IRSNGIEASL LTDPKDVSGR TVDYIIAGGG LTGLTTAARL 

        70         80         90        100        110        120 
TENPNISVLV IESGSYESDR GPIIEDLNAY GDIFGSSVDH AYETVELATN NQTALIRSGN 

       130        140        150        160        170        180 
GLGGSTLVNG GTWTRPHKAQ VDSWETVFGN EGWNWDNVAA YSLQAERARA PNAKQIAAGH 

       190        200        210        220        230        240 
YFNASCHGVN GTVHAGPRDT GDDYSPIVKA LMSAVEDRGV PTKKDFGCGD PHGVSMFPNT 

       250        260        270        280        290        300 
LHEDQVRSDA AREWLLPNYQ RPNLQVLTGQ YVGKVLLSQN GTTPRAVGVE FGTHKGNTHN 

       310        320        330        340        350        360 
VYAKHEVLLA AGSAVSPTIL EYSGIGMKSI LEPLGIDTVV DLPVGLNLQD QTTATVRSRI 

       370        380        390        400        410        420 
TSAGAGQGQA AWFATFNETF GDYSEKAHEL LNTKLEQWAE EAVARGGFHN TTALLIQYEN 

       430        440        450        460        470        480 
YRDWIVNHNV AYSELFLDTA GVASFDVWDL LPFTRGYVHI LDKDPYLHHF AYDPQYFLNE 

       490        500        510        520        530        540 
LDLLGQAAAT QLARNISNSG AMQTYFAGET IPGDNLAYDA DLSAWTEYIP YHFRPNYHGV 

       550        560        570        580        590        600 
GTCSMMPKEM GGVVDNAARV YGVQGLRVID GSIPPTQMSS HVMTVFYAMA LKISDAILED 


YASMQ

« Hide

References

[1]"Cloning and DNA sequence analysis of the glucose oxidase gene from Aspergillus niger NRRL-3."
Kriechbaum M., Heilmann H.J., Wientjes F.J., Hahn M., Jany K.-D., Gassen H.G., Sharif F., Alaeddinoglu G.
FEBS Lett. 255:63-66(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived enzyme."
Frederick K.R., Tung J., Emerick R.S., Masiarz F.R., Chamberlain S.H., Vasavada A., Rosenberg S., Chakraborty S., Schopter L.M., Massey V.
J. Biol. Chem. 265:3793-3802(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Expression of the Aspergillus niger glucose oxidase gene in A. niger, A. nidulans and Saccharomyces cerevisiae."
Whittington H., Kerry-Williams S., Bidgood K., Dodsworth N., Peberdy J., Dobson M., Hinchliffe E., Ballance D.J.
Curr. Genet. 18:531-536(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-32.
[4]"Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3-A resolution."
Hecht H.-J., Kalisz H.M., Hendle J., Schmid R.D., Schomburg D.
J. Mol. Biol. 229:153-172(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[5]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X16061 Genomic DNA. Translation: CAA34197.1.
J05242 mRNA. Translation: AAA32695.1.
X56443 Genomic DNA. Translation: CAA39826.1.
PIRA35459.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF3X-ray1.90A23-605[»]
1GALX-ray2.30A23-605[»]
3QVPX-ray1.20A23-605[»]
3QVRX-ray1.30A23-605[»]
ProteinModelPortalP13006.
SMRP13006. Positions 25-605.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2303.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17584.
SABIO-RKP13006.

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...

Other

EvolutionaryTraceP13006.

Entry information

Entry nameGOX_ASPNG
AccessionPrimary (citable) accession number: P13006
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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