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Protein

Glucose oxidase

Gene
N/A
Organism
Penicillium amagasakiense
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei520Proton acceptorBy similarity1

Regions

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.3.4. 4597.
SABIO-RKP81156.

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

GO - Cellular componenti

Complete GO annotation...

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...)By 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Helixi17 – 19Combined sources3
Turni20 – 22Combined sources3
Beta strandi24 – 30Combined sources7
Helixi34 – 44Combined sources11
Beta strandi51 – 57Combined sources7
Helixi65 – 68Combined sources4
Helixi70 – 72Combined sources3
Turni73 – 78Combined sources6
Helixi106 – 109Combined sources4
Helixi120 – 128Combined sources9
Helixi137 – 146Combined sources10
Beta strandi148 – 150Combined sources3
Helixi155 – 160Combined sources6
Helixi166 – 168Combined sources3
Beta strandi171 – 178Combined sources8
Helixi189 – 199Combined sources11
Beta strandi215 – 217Combined sources3
Beta strandi220 – 223Combined sources4
Helixi232 – 236Combined sources5
Turni237 – 242Combined sources6
Beta strandi246 – 251Combined sources6
Beta strandi253 – 262Combined sources10
Beta strandi265 – 276Combined sources12
Beta strandi279 – 291Combined sources13
Turni295 – 297Combined sources3
Helixi298 – 304Combined sources7
Helixi310 – 315Combined sources6
Beta strandi321 – 323Combined sources3
Beta strandi329 – 331Combined sources3
Beta strandi334 – 342Combined sources9
Helixi344 – 346Combined sources3
Beta strandi351 – 357Combined sources7
Helixi358 – 362Combined sources5
Helixi363 – 365Combined sources3
Helixi366 – 375Combined sources10
Helixi377 – 386Combined sources10
Helixi393 – 409Combined sources17
Beta strandi413 – 420Combined sources8
Beta strandi424 – 433Combined sources10
Beta strandi438 – 445Combined sources8
Helixi447 – 449Combined sources3
Beta strandi452 – 455Combined sources4
Helixi462 – 479Combined sources18
Helixi484 – 487Combined sources4
Beta strandi488 – 494Combined sources7
Helixi495 – 497Combined sources3
Helixi504 – 513Combined sources10
Helixi530 – 532Combined sources3
Beta strandi546 – 550Combined sources5
Helixi565 – 585Combined sources21

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...

Miscellaneous databases

EvolutionaryTraceiP81156.

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
4.10.450.10. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR027424. 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.
SUPFAMiSSF51905. SSF51905. 2 hits.
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
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-RKP81156.

Miscellaneous databases

EvolutionaryTraceiP81156.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
4.10.450.10. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR027424. 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.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 84 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.