GOX_PENAG
ID GOX_PENAG Reviewed; 587 AA.
AC P81156;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glucose oxidase;
DE EC=1.1.3.4;
DE AltName: Full=Beta-D-glucose:oxygen 1-oxido-reductase;
DE AltName: Full=Glucose oxyhydrase;
DE Short=GOD;
OS Penicillium amagasakiense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=63559;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=9523716; DOI=10.1046/j.1432-1327.1998.2520090.x;
RA Kiess M., Hecht H.-J., Kalisz H.M.;
RT "Glucose oxidase from Penicillium amagasakiense. Primary structure and
RT comparison with other glucose-methanol-choline (GMC) oxidoreductases.";
RL Eur. J. Biochem. 252:90-99(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10216293; DOI=10.1107/s0907444999003431;
RA Wohlfahrt G., Witt S., Hendle J., Schomburg D., Kalisz H.M., Hecht H.-J.;
RT "1.8 and 1.9-A resolution structures of the Penicillium amagasakiense and
RT Aspergillus niger glucose oxidases as a basis for modelling substrate
RT complexes.";
RL Acta Crystallogr. D 55:969-977(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2;
CC Xref=Rhea:RHEA:11428, ChEBI:CHEBI:15379, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:16240; EC=1.1.3.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: This enzyme is widely applied for the determination of
CC glucose in body fluids and in removing residual glucose or oxygen from
CC foods and beverages. Furthermore, glucose oxidase-producing moulds such
CC as aspergillus and penicillium species are used for the biological
CC production of gluconic acid.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR PDB; 1GPE; X-ray; 1.80 A; A/B=1-587.
DR PDBsum; 1GPE; -.
DR AlphaFoldDB; P81156; -.
DR SMR; P81156; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR BRENDA; 1.1.3.4; 4597.
DR SABIO-RK; P81156; -.
DR EvolutionaryTrace; P81156; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046562; F:glucose oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 4.10.450.10; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycoprotein; Oxidoreductase; Secreted.
FT CHAIN 1..587
FT /note="Glucose oxidase"
FT /id="PRO_0000205611"
FT ACT_SITE 520
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 26..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 168..210
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1GPE"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1GPE"
FT TURN 73..78
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1GPE"
FT TURN 237..242
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 265..276
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 279..291
FT /evidence="ECO:0007829|PDB:1GPE"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 413..420
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 424..433
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 462..479
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 484..487
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 504..513
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:1GPE"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:1GPE"
FT HELIX 565..585
FT /evidence="ECO:0007829|PDB:1GPE"
SQ SEQUENCE 587 AA; 63965 MW; 2827477B3DF4508C CRC64;
YLPAQQIDVQ SSLLSDPSKV AGKTYDYIIA GGGLTGLTVA AKLTENPKIK VLVIEKGFYE
SNDGAIIEDP NAYGQIFGTT VDQNYLTVPL INNRTNNIKA GKGLGGSTLI NGDSWTRPDK
VQIDSWEKVF GMEGWNWDNM FEYMKKAEAA RTPTAAQLAA GHSFNATCHG TNGTVQSGAR
DNGQPWSPIM KALMNTVSAL GVPVQQDFLC GHPRGVSMIM NNLDENQVRV DAARAWLLPN
YQRSNLEILT GQMVGKVLFK QTASGPQAVG VNFGTNKAVN FDVFAKHEVL LAAGSAISPL
ILEYSGIGLK SVLDQANVTQ LLDLPVGINM QDQTTTTVSS RASSAGAGQG QAVFFANFTE
TFGDYAPQAR DLLNTKLDQW AEETVARGGF HNVTALKVQY ENYRNWLLDE DVAFAELFMD
TEGKINFDLW DLIPFTRGSV HILSSDPYLW QFANDPKFFL NEFDLLGQAA ASKLARDLTS
QGAMKEYFAG ETLPGYNLVQ NATLSQWSDY VLQNFRPNWH AVSSCSMMSR ELGGVVDATA
KVYGTQGLRV IDGSIPPTQV SSHVMTIFYG MALKVADAIL DDYAKSA
