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Protein

Glucose oxidase

Gene

gox

Organism
Aspergillus niger
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 sitei538Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 72FADCuratedAdd BLAST30

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17584.
BRENDAi1.1.3.4. 518.
SABIO-RKP13006.

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
Gene namesi
Name:gox
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Or 48Add BLAST22
ChainiPRO_000001233823 – 605Glucose oxidaseAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...)1
Disulfide bondi186 ↔ 228

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP13006.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi5061.CADANGAP00001413.

Structurei

Secondary structure

1605
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 29Combined sources4
Helixi34 – 36Combined sources3
Turni37 – 39Combined sources3
Beta strandi41 – 47Combined sources7
Helixi51 – 60Combined sources10
Beta strandi68 – 71Combined sources4
Helixi82 – 85Combined sources4
Helixi87 – 89Combined sources3
Turni90 – 95Combined sources6
Turni108 – 110Combined sources3
Helixi124 – 127Combined sources4
Helixi138 – 146Combined sources9
Helixi155 – 165Combined sources11
Beta strandi166 – 168Combined sources3
Helixi173 – 178Combined sources6
Helixi184 – 186Combined sources3
Beta strandi189 – 196Combined sources8
Helixi207 – 216Combined sources10
Turni217 – 219Combined sources3
Beta strandi233 – 235Combined sources3
Beta strandi239 – 241Combined sources3
Helixi250 – 254Combined sources5
Turni255 – 260Combined sources6
Beta strandi264 – 267Combined sources4
Beta strandi271 – 278Combined sources8
Beta strandi280 – 283Combined sources4
Beta strandi285 – 294Combined sources10
Beta strandi298 – 309Combined sources12
Turni313 – 315Combined sources3
Helixi316 – 322Combined sources7
Helixi328 – 331Combined sources4
Helixi332 – 334Combined sources3
Beta strandi339 – 341Combined sources3
Beta strandi346 – 349Combined sources4
Beta strandi352 – 360Combined sources9
Helixi362 – 364Combined sources3
Beta strandi369 – 375Combined sources7
Helixi376 – 380Combined sources5
Helixi381 – 383Combined sources3
Helixi384 – 393Combined sources10
Helixi395 – 404Combined sources10
Helixi411 – 427Combined sources17
Beta strandi431 – 438Combined sources8
Beta strandi442 – 451Combined sources10
Beta strandi456 – 463Combined sources8
Helixi465 – 467Combined sources3
Beta strandi470 – 473Combined sources4
Helixi480 – 497Combined sources18
Helixi502 – 505Combined sources4
Beta strandi506 – 512Combined sources7
Helixi513 – 515Combined sources3
Helixi522 – 528Combined sources7
Helixi529 – 531Combined sources3
Helixi548 – 550Combined sources3
Beta strandi558 – 560Combined sources3
Beta strandi564 – 568Combined sources5
Helixi583 – 603Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CF3X-ray1.90A23-605[»]
1GALX-ray2.30A23-605[»]
3QVPX-ray1.20A23-605[»]
3QVRX-ray1.30A23-605[»]
ProteinModelPortaliP13006.
SMRiP13006.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13006.

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1238. Eukaryota.
COG2303. LUCA.

Family and domain databases

Gene3Di3.50.50.60. 3 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTLLVSSLV VSLAAALPHY IRSNGIEASL LTDPKDVSGR TVDYIIAGGG
60 70 80 90 100
LTGLTTAARL TENPNISVLV IESGSYESDR GPIIEDLNAY GDIFGSSVDH
110 120 130 140 150
AYETVELATN NQTALIRSGN GLGGSTLVNG GTWTRPHKAQ VDSWETVFGN
160 170 180 190 200
EGWNWDNVAA YSLQAERARA PNAKQIAAGH YFNASCHGVN GTVHAGPRDT
210 220 230 240 250
GDDYSPIVKA LMSAVEDRGV PTKKDFGCGD PHGVSMFPNT LHEDQVRSDA
260 270 280 290 300
AREWLLPNYQ RPNLQVLTGQ YVGKVLLSQN GTTPRAVGVE FGTHKGNTHN
310 320 330 340 350
VYAKHEVLLA AGSAVSPTIL EYSGIGMKSI LEPLGIDTVV DLPVGLNLQD
360 370 380 390 400
QTTATVRSRI TSAGAGQGQA AWFATFNETF GDYSEKAHEL LNTKLEQWAE
410 420 430 440 450
EAVARGGFHN TTALLIQYEN YRDWIVNHNV AYSELFLDTA GVASFDVWDL
460 470 480 490 500
LPFTRGYVHI LDKDPYLHHF AYDPQYFLNE LDLLGQAAAT QLARNISNSG
510 520 530 540 550
AMQTYFAGET IPGDNLAYDA DLSAWTEYIP YHFRPNYHGV GTCSMMPKEM
560 570 580 590 600
GGVVDNAARV YGVQGLRVID GSIPPTQMSS HVMTVFYAMA LKISDAILED

YASMQ
Length:605
Mass (Da):65,638
Last modified:January 1, 1990 - v1
Checksum:i25243E5ED1D2773B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16061 Genomic DNA. Translation: CAA34197.1.
J05242 mRNA. Translation: AAA32695.1.
X56443 Genomic DNA. Translation: CAA39826.1.
PIRiA35459.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16061 Genomic DNA. Translation: CAA34197.1.
J05242 mRNA. Translation: AAA32695.1.
X56443 Genomic DNA. Translation: CAA39826.1.
PIRiA35459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CF3X-ray1.90A23-605[»]
1GALX-ray2.30A23-605[»]
3QVPX-ray1.20A23-605[»]
3QVRX-ray1.30A23-605[»]
ProteinModelPortaliP13006.
SMRiP13006.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00001413.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

Proteomic databases

PaxDbiP13006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1238. Eukaryota.
COG2303. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17584.
BRENDAi1.1.3.4. 518.
SABIO-RKP13006.

Miscellaneous databases

EvolutionaryTraceiP13006.

Family and domain databases

Gene3Di3.50.50.60. 3 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_ASPNG
AccessioniPrimary (citable) accession number: P13006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 111 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 molds 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.