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Protein

Glucose oxidase

Gene
N/A
Organism
Penicillium amagasakiense
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei520Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi26 – 55FADCuratedAdd BLAST30

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.3.4 4597
SABIO-RKiP81156

Protein family/group databases

CAZyiAA3 Auxiliary Activities 3

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose oxidase (EC:1.1.3.4)
Alternative name(s):
Beta-D-glucose:oxygen 1-oxido-reductase
Glucose oxyhydrase
Short name:
GOD
OrganismiPenicillium amagasakiense
Taxonomic identifieri63559 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002056111 – 587Glucose oxidaseAdd BLAST587

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi93N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi168 ↔ 210

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1587
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP81156
SMRiP81156
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81156

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Family and domain databases

Gene3Di3.50.50.60, 1 hit
4.10.450.10, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR027424 Glucose_Oxidase_domain_2
IPR012132 GMC_OxRdtase
IPR000172 GMC_OxRdtase_N
IPR007867 GMC_OxRtase_C
PfamiView protein in Pfam
PF05199 GMC_oxred_C, 1 hit
PF00732 GMC_oxred_N, 1 hit
PIRSFiPIRSF000137 Alcohol_oxidase, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00623 GMC_OXRED_1, 1 hit
PS00624 GMC_OXRED_2, 1 hit

Sequencei

Sequence statusi: Complete.

P81156-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
YLPAQQIDVQ SSLLSDPSKV AGKTYDYIIA GGGLTGLTVA AKLTENPKIK
60 70 80 90 100
VLVIEKGFYE SNDGAIIEDP NAYGQIFGTT VDQNYLTVPL INNRTNNIKA
110 120 130 140 150
GKGLGGSTLI NGDSWTRPDK VQIDSWEKVF GMEGWNWDNM FEYMKKAEAA
160 170 180 190 200
RTPTAAQLAA GHSFNATCHG TNGTVQSGAR DNGQPWSPIM KALMNTVSAL
210 220 230 240 250
GVPVQQDFLC GHPRGVSMIM NNLDENQVRV DAARAWLLPN YQRSNLEILT
260 270 280 290 300
GQMVGKVLFK QTASGPQAVG VNFGTNKAVN FDVFAKHEVL LAAGSAISPL
310 320 330 340 350
ILEYSGIGLK SVLDQANVTQ LLDLPVGINM QDQTTTTVSS RASSAGAGQG
360 370 380 390 400
QAVFFANFTE TFGDYAPQAR DLLNTKLDQW AEETVARGGF HNVTALKVQY
410 420 430 440 450
ENYRNWLLDE DVAFAELFMD TEGKINFDLW DLIPFTRGSV HILSSDPYLW
460 470 480 490 500
QFANDPKFFL NEFDLLGQAA ASKLARDLTS QGAMKEYFAG ETLPGYNLVQ
510 520 530 540 550
NATLSQWSDY VLQNFRPNWH AVSSCSMMSR ELGGVVDATA KVYGTQGLRV
560 570 580
IDGSIPPTQV SSHVMTIFYG MALKVADAIL DDYAKSA
Length:587
Mass (Da):63,965
Last modified:July 15, 1998 - v1
Checksum:i2827477B3DF4508C
GO

Similar proteinsi

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPEX-ray1.80A/B1-587[»]
ProteinModelPortaliP81156
SMRiP81156
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA3 Auxiliary Activities 3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.3.4 4597
SABIO-RKiP81156

Miscellaneous databases

EvolutionaryTraceiP81156

Family and domain databases

Gene3Di3.50.50.60, 1 hit
4.10.450.10, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR027424 Glucose_Oxidase_domain_2
IPR012132 GMC_OxRdtase
IPR000172 GMC_OxRdtase_N
IPR007867 GMC_OxRtase_C
PfamiView protein in Pfam
PF05199 GMC_oxred_C, 1 hit
PF00732 GMC_oxred_N, 1 hit
PIRSFiPIRSF000137 Alcohol_oxidase, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00623 GMC_OXRED_1, 1 hit
PS00624 GMC_OXRED_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGOX_PENAG
AccessioniPrimary (citable) accession number: P81156
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 7, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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