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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

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 5530FADCuratedAdd
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-KW
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 – 123Combined sources
Helixi17 – 193Combined sources
Turni20 – 223Combined sources
Beta strandi24 – 307Combined sources
Helixi34 – 4411Combined sources
Beta strandi51 – 577Combined sources
Helixi65 – 684Combined sources
Helixi70 – 723Combined sources
Turni73 – 786Combined sources
Helixi106 – 1094Combined sources
Helixi120 – 1289Combined sources
Helixi137 – 14610Combined sources
Beta strandi148 – 1503Combined sources
Helixi155 – 1606Combined sources
Helixi166 – 1683Combined sources
Beta strandi171 – 1788Combined sources
Helixi189 – 19911Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi220 – 2234Combined sources
Helixi232 – 2365Combined sources
Turni237 – 2426Combined sources
Beta strandi246 – 2516Combined sources
Beta strandi253 – 26210Combined sources
Beta strandi265 – 27612Combined sources
Beta strandi279 – 29113Combined sources
Turni295 – 2973Combined sources
Helixi298 – 3047Combined sources
Helixi310 – 3156Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi334 – 3429Combined sources
Helixi344 – 3463Combined sources
Beta strandi351 – 3577Combined sources
Helixi358 – 3625Combined sources
Helixi363 – 3653Combined sources
Helixi366 – 37510Combined sources
Helixi377 – 38610Combined sources
Helixi393 – 40917Combined sources
Beta strandi413 – 4208Combined sources
Beta strandi424 – 43310Combined sources
Beta strandi438 – 4458Combined sources
Helixi447 – 4493Combined sources
Beta strandi452 – 4554Combined sources
Helixi462 – 47918Combined sources
Helixi484 – 4874Combined sources
Beta strandi488 – 4947Combined sources
Helixi495 – 4973Combined sources
Helixi504 – 51310Combined sources
Helixi530 – 5323Combined sources
Beta strandi546 – 5505Combined sources
Helixi565 – 58521Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP81156.

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

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

        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

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 26, 2014
This is version 73 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