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P13006

- GOX_ASPNG

UniProt

P13006 - GOX_ASPNG

Protein

Glucose oxidase

Gene

gox

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2.

    Cofactori

    FAD.

    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

    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

    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.
    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

    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: October 1, 2014
    This is version 98 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