SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P13006

- GOX_ASPNG

UniProt

P13006 - GOX_ASPNG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucose oxidase

Gene
gox
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 5 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 sitei538 – 5381 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 7230FAD 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

BioCyciMetaCyc:MONOMER-17584.
SABIO-RKP13006.

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

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Or 48Add
BLAST
Chaini23 – 605583Glucose oxidasePRO_0000012338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)
Disulfide bondi186 ↔ 228

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
605
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 294
Helixi34 – 363
Turni37 – 393
Beta strandi41 – 477
Helixi51 – 6010
Beta strandi68 – 714
Helixi82 – 854
Helixi87 – 893
Turni90 – 956
Turni108 – 1103
Helixi124 – 1274
Helixi138 – 1469
Helixi155 – 16511
Beta strandi166 – 1683
Helixi173 – 1786
Helixi184 – 1863
Beta strandi189 – 1968
Helixi207 – 21610
Turni217 – 2193
Beta strandi233 – 2353
Beta strandi239 – 2413
Helixi250 – 2545
Turni255 – 2606
Beta strandi264 – 2674
Beta strandi271 – 2788
Beta strandi280 – 2834
Beta strandi285 – 29410
Beta strandi298 – 30912
Turni313 – 3153
Helixi316 – 3227
Helixi328 – 3314
Helixi332 – 3343
Beta strandi339 – 3413
Beta strandi346 – 3494
Beta strandi352 – 3609
Helixi362 – 3643
Beta strandi369 – 3757
Helixi376 – 3805
Helixi381 – 3833
Helixi384 – 39310
Helixi395 – 40410
Helixi411 – 42717
Beta strandi431 – 4388
Beta strandi442 – 45110
Beta strandi456 – 4638
Helixi465 – 4673
Beta strandi470 – 4734
Helixi480 – 49718
Helixi502 – 5054
Beta strandi506 – 5127
Helixi513 – 5153
Helixi522 – 5287
Helixi529 – 5313
Helixi548 – 5503
Beta strandi558 – 5603
Beta strandi564 – 5685
Helixi583 – 60321

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF3X-ray1.90A23-605[»]
1GALX-ray2.30A23-605[»]
3QVPX-ray1.20A23-605[»]
3QVRX-ray1.30A23-605[»]
ProteinModelPortaliP13006.
SMRiP13006. Positions 25-605.

Miscellaneous databases

EvolutionaryTraceiP13006.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2303.

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.

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

P13006-1 [UniParc]FASTAAdd to Basket

« Hide

MQTLLVSSLV VSLAAALPHY IRSNGIEASL LTDPKDVSGR TVDYIIAGGG    50
LTGLTTAARL TENPNISVLV IESGSYESDR GPIIEDLNAY GDIFGSSVDH 100
AYETVELATN NQTALIRSGN GLGGSTLVNG GTWTRPHKAQ VDSWETVFGN 150
EGWNWDNVAA YSLQAERARA PNAKQIAAGH YFNASCHGVN GTVHAGPRDT 200
GDDYSPIVKA LMSAVEDRGV PTKKDFGCGD PHGVSMFPNT LHEDQVRSDA 250
AREWLLPNYQ RPNLQVLTGQ YVGKVLLSQN GTTPRAVGVE FGTHKGNTHN 300
VYAKHEVLLA AGSAVSPTIL EYSGIGMKSI LEPLGIDTVV DLPVGLNLQD 350
QTTATVRSRI TSAGAGQGQA AWFATFNETF GDYSEKAHEL LNTKLEQWAE 400
EAVARGGFHN TTALLIQYEN YRDWIVNHNV AYSELFLDTA GVASFDVWDL 450
LPFTRGYVHI LDKDPYLHHF AYDPQYFLNE LDLLGQAAAT QLARNISNSG 500
AMQTYFAGET IPGDNLAYDA DLSAWTEYIP YHFRPNYHGV GTCSMMPKEM 550
GGVVDNAARV YGVQGLRVID GSIPPTQMSS HVMTVFYAMA LKISDAILED 600
YASMQ 605
Length:605
Mass (Da):65,638
Last modified:January 1, 1990 - v1
Checksum:i25243E5ED1D2773B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X16061 Genomic DNA. Translation: CAA34197.1 .
J05242 mRNA. Translation: AAA32695.1 .
X56443 Genomic DNA. Translation: CAA39826.1 .
PIRi A35459.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CF3 X-ray 1.90 A 23-605 [» ]
1GAL X-ray 2.30 A 23-605 [» ]
3QVP X-ray 1.20 A 23-605 [» ]
3QVR X-ray 1.30 A 23-605 [» ]
ProteinModelPortali P13006.
SMRi P13006. Positions 25-605.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2303.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17584.
SABIO-RK P13006.

Miscellaneous databases

EvolutionaryTracei P13006.

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. "Cloning and DNA sequence analysis of the glucose oxidase gene from Aspergillus niger NRRL-3."
    Kriechbaum M., Heilmann H.J., Wientjes F.J., Hahn M., Jany K.-D., Gassen H.G., Sharif F., Alaeddinoglu G.
    FEBS Lett. 255:63-66(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. "Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived enzyme."
    Frederick K.R., Tung J., Emerick R.S., Masiarz F.R., Chamberlain S.H., Vasavada A., Rosenberg S., Chakraborty S., Schopter L.M., Massey V.
    J. Biol. Chem. 265:3793-3802(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Expression of the Aspergillus niger glucose oxidase gene in A. niger, A. nidulans and Saccharomyces cerevisiae."
    Whittington H., Kerry-Williams S., Bidgood K., Dodsworth N., Peberdy J., Dobson M., Hinchliffe E., Ballance D.J.
    Curr. Genet. 18:531-536(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-32.
  4. "Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3-A resolution."
    Hecht H.-J., Kalisz H.M., Hendle J., Schmid R.D., Schomburg D.
    J. Mol. Biol. 229:153-172(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  5. "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 (1.9 ANGSTROMS).

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 13, 2013
This is version 97 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

External Data

Dasty 3

Similar proteinsi