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P13006

- GOX_ASPNG

UniProt

P13006 - GOX_ASPNG

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Protein

Glucose oxidase

Gene

gox

Organism
Aspergillus niger
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 sitei538 – 5381By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 7230FADCuratedAdd
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-KW
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 – 294Combined sources
Helixi34 – 363Combined sources
Turni37 – 393Combined sources
Beta strandi41 – 477Combined sources
Helixi51 – 6010Combined sources
Beta strandi68 – 714Combined sources
Helixi82 – 854Combined sources
Helixi87 – 893Combined sources
Turni90 – 956Combined sources
Turni108 – 1103Combined sources
Helixi124 – 1274Combined sources
Helixi138 – 1469Combined sources
Helixi155 – 16511Combined sources
Beta strandi166 – 1683Combined sources
Helixi173 – 1786Combined sources
Helixi184 – 1863Combined sources
Beta strandi189 – 1968Combined sources
Helixi207 – 21610Combined sources
Turni217 – 2193Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi239 – 2413Combined sources
Helixi250 – 2545Combined sources
Turni255 – 2606Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi271 – 2788Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi285 – 29410Combined sources
Beta strandi298 – 30912Combined sources
Turni313 – 3153Combined sources
Helixi316 – 3227Combined sources
Helixi328 – 3314Combined sources
Helixi332 – 3343Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi346 – 3494Combined sources
Beta strandi352 – 3609Combined sources
Helixi362 – 3643Combined sources
Beta strandi369 – 3757Combined sources
Helixi376 – 3805Combined sources
Helixi381 – 3833Combined sources
Helixi384 – 39310Combined sources
Helixi395 – 40410Combined sources
Helixi411 – 42717Combined sources
Beta strandi431 – 4388Combined sources
Beta strandi442 – 45110Combined sources
Beta strandi456 – 4638Combined sources
Helixi465 – 4673Combined sources
Beta strandi470 – 4734Combined sources
Helixi480 – 49718Combined sources
Helixi502 – 5054Combined sources
Beta strandi506 – 5127Combined sources
Helixi513 – 5153Combined sources
Helixi522 – 5287Combined sources
Helixi529 – 5313Combined sources
Helixi548 – 5503Combined sources
Beta strandi558 – 5603Combined sources
Beta strandi564 – 5685Combined sources
Helixi583 – 60321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13006.

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

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

        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 .
PIRi A35459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 26, 2014
This is version 100 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