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 27-MAR-2024, entry version 102. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; FAD/NAD(P)-binding domain; 1. DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1. DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1. DR PANTHER; PTHR11552:SF201; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR PIRSF; PIRSF000137; Alcohol_oxidase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 //