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P81156

- GOX_PENAG

UniProt

P81156 - GOX_PENAG

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Protein

Glucose oxidase

Gene
N/A
Organism
Penicillium amagasakiense
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei520 – 5201

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 5530FAD InferredAdd
BLAST

GO - Molecular functioni

  1. choline dehydrogenase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. glucose oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. alcohol metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKP81156.

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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 587587Glucose oxidasePRO_0000205611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...) By similarity
Disulfide bondi168 ↔ 210

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
587
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123
Helixi17 – 193
Turni20 – 223
Beta strandi24 – 307
Helixi34 – 4411
Beta strandi51 – 577
Helixi65 – 684
Helixi70 – 723
Turni73 – 786
Helixi106 – 1094
Helixi120 – 1289
Helixi137 – 14610
Beta strandi148 – 1503
Helixi155 – 1606
Helixi166 – 1683
Beta strandi171 – 1788
Helixi189 – 19911
Beta strandi215 – 2173
Beta strandi220 – 2234
Helixi232 – 2365
Turni237 – 2426
Beta strandi246 – 2516
Beta strandi253 – 26210
Beta strandi265 – 27612
Beta strandi279 – 29113
Turni295 – 2973
Helixi298 – 3047
Helixi310 – 3156
Beta strandi321 – 3233
Beta strandi329 – 3313
Beta strandi334 – 3429
Helixi344 – 3463
Beta strandi351 – 3577
Helixi358 – 3625
Helixi363 – 3653
Helixi366 – 37510
Helixi377 – 38610
Helixi393 – 40917
Beta strandi413 – 4208
Beta strandi424 – 43310
Beta strandi438 – 4458
Helixi447 – 4493
Beta strandi452 – 4554
Helixi462 – 47918
Helixi484 – 4874
Beta strandi488 – 4947
Helixi495 – 4973
Helixi504 – 51310
Helixi530 – 5323
Beta strandi546 – 5505
Helixi565 – 58521

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPEX-ray1.80A/B1-587[»]
ProteinModelPortaliP81156.
SMRiP81156. Positions 1-587.

Miscellaneous databases

EvolutionaryTraceiP81156.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di4.10.450.10. 1 hit.
InterProiIPR027424. Glucose_Oxidase_domain_2.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81156-1 [UniParc]FASTAAdd to Basket

« Hide

YLPAQQIDVQ SSLLSDPSKV AGKTYDYIIA GGGLTGLTVA AKLTENPKIK    50
VLVIEKGFYE SNDGAIIEDP NAYGQIFGTT VDQNYLTVPL INNRTNNIKA 100
GKGLGGSTLI NGDSWTRPDK VQIDSWEKVF GMEGWNWDNM FEYMKKAEAA 150
RTPTAAQLAA GHSFNATCHG TNGTVQSGAR DNGQPWSPIM KALMNTVSAL 200
GVPVQQDFLC GHPRGVSMIM NNLDENQVRV DAARAWLLPN YQRSNLEILT 250
GQMVGKVLFK QTASGPQAVG VNFGTNKAVN FDVFAKHEVL LAAGSAISPL 300
ILEYSGIGLK SVLDQANVTQ LLDLPVGINM QDQTTTTVSS RASSAGAGQG 350
QAVFFANFTE TFGDYAPQAR DLLNTKLDQW AEETVARGGF HNVTALKVQY 400
ENYRNWLLDE DVAFAELFMD TEGKINFDLW DLIPFTRGSV HILSSDPYLW 450
QFANDPKFFL NEFDLLGQAA ASKLARDLTS QGAMKEYFAG ETLPGYNLVQ 500
NATLSQWSDY VLQNFRPNWH AVSSCSMMSR ELGGVVDATA KVYGTQGLRV 550
IDGSIPPTQV SSHVMTIFYG MALKVADAIL DDYAKSA 587
Length:587
Mass (Da):63,965
Last modified:July 15, 1998 - v1
Checksum:i2827477B3DF4508C
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GPE X-ray 1.80 A/B 1-587 [» ]
ProteinModelPortali P81156.
SMRi P81156. Positions 1-587.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P81156.

Miscellaneous databases

EvolutionaryTracei P81156.

Family and domain databases

Gene3Di 4.10.450.10. 1 hit.
InterProi IPR027424. Glucose_Oxidase_domain_2.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view ]
Pfami PF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000137. Alcohol_oxidase. 1 hit.
PROSITEi PS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiGOX_PENAG
AccessioniPrimary (citable) accession number: P81156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 13, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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