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P81156

- GOX_PENAG

UniProt

P81156 - GOX_PENAG

Protein

Glucose oxidase

Gene
N/A
Organism
Penicillium amagasakiense
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      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 sitei520 – 5201

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 5530FADCuratedAdd
    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

    SABIO-RKP81156.

    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

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 587587Glucose oxidasePRO_0000205611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi93 – 931N-linked (GlcNAc...)By similarity
    Disulfide bondi168 ↔ 210

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    587
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 123
    Helixi17 – 193
    Turni20 – 223
    Beta strandi24 – 307
    Helixi34 – 4411
    Beta strandi51 – 577
    Helixi65 – 684
    Helixi70 – 723
    Turni73 – 786
    Helixi106 – 1094
    Helixi120 – 1289
    Helixi137 – 14610
    Beta strandi148 – 1503
    Helixi155 – 1606
    Helixi166 – 1683
    Beta strandi171 – 1788
    Helixi189 – 19911
    Beta strandi215 – 2173
    Beta strandi220 – 2234
    Helixi232 – 2365
    Turni237 – 2426
    Beta strandi246 – 2516
    Beta strandi253 – 26210
    Beta strandi265 – 27612
    Beta strandi279 – 29113
    Turni295 – 2973
    Helixi298 – 3047
    Helixi310 – 3156
    Beta strandi321 – 3233
    Beta strandi329 – 3313
    Beta strandi334 – 3429
    Helixi344 – 3463
    Beta strandi351 – 3577
    Helixi358 – 3625
    Helixi363 – 3653
    Helixi366 – 37510
    Helixi377 – 38610
    Helixi393 – 40917
    Beta strandi413 – 4208
    Beta strandi424 – 43310
    Beta strandi438 – 4458
    Helixi447 – 4493
    Beta strandi452 – 4554
    Helixi462 – 47918
    Helixi484 – 4874
    Beta strandi488 – 4947
    Helixi495 – 4973
    Helixi504 – 51310
    Helixi530 – 5323
    Beta strandi546 – 5505
    Helixi565 – 58521

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GPEX-ray1.80A/B1-587[»]
    ProteinModelPortaliP81156.
    SMRiP81156. Positions 1-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81156.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    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.

    P81156-1 [UniParc]FASTAAdd to Basket

    « Hide

    YLPAQQIDVQ SSLLSDPSKV AGKTYDYIIA GGGLTGLTVA AKLTENPKIK    50
    VLVIEKGFYE SNDGAIIEDP NAYGQIFGTT VDQNYLTVPL INNRTNNIKA 100
    GKGLGGSTLI NGDSWTRPDK VQIDSWEKVF GMEGWNWDNM FEYMKKAEAA 150
    RTPTAAQLAA GHSFNATCHG TNGTVQSGAR DNGQPWSPIM KALMNTVSAL 200
    GVPVQQDFLC GHPRGVSMIM NNLDENQVRV DAARAWLLPN YQRSNLEILT 250
    GQMVGKVLFK QTASGPQAVG VNFGTNKAVN FDVFAKHEVL LAAGSAISPL 300
    ILEYSGIGLK SVLDQANVTQ LLDLPVGINM QDQTTTTVSS RASSAGAGQG 350
    QAVFFANFTE TFGDYAPQAR DLLNTKLDQW AEETVARGGF HNVTALKVQY 400
    ENYRNWLLDE DVAFAELFMD TEGKINFDLW DLIPFTRGSV HILSSDPYLW 450
    QFANDPKFFL NEFDLLGQAA ASKLARDLTS QGAMKEYFAG ETLPGYNLVQ 500
    NATLSQWSDY VLQNFRPNWH AVSSCSMMSR ELGGVVDATA KVYGTQGLRV 550
    IDGSIPPTQV SSHVMTIFYG MALKVADAIL DDYAKSA 587
    Length:587
    Mass (Da):63,965
    Last modified:July 15, 1998 - v1
    Checksum:i2827477B3DF4508C
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GPE X-ray 1.80 A/B 1-587 [» ]
    ProteinModelPortali P81156.
    SMRi P81156. Positions 1-587.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P81156.

    Miscellaneous databases

    EvolutionaryTracei P81156.

    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. "Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases."
      Kiess M., Hecht H.-J., Kalisz H.M.
      Eur. J. Biochem. 252:90-99(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "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 (1.8 ANGSTROMS).

    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: October 1, 2014
    This is version 71 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

    External Data

    Dasty 3