GOX_ASPNG
ID GOX_ASPNG Reviewed; 605 AA.
AC P13006;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 135.
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;
DE Flags: Precursor;
GN Name=gox;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=2792372; DOI=10.1016/0014-5793(89)81061-0;
RA Kriechbaum M., Heilmann H.J., Wientjes F.J., Hahn M., Jany K.-D.,
RA Gassen H.G., Sharif F., Alaeddinoglu G.;
RT "Cloning and DNA sequence analysis of the glucose oxidase gene from
RT Aspergillus niger NRRL-3.";
RL FEBS Lett. 255:63-66(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2406261; DOI=10.1016/s0021-9258(19)39664-4;
RA Frederick K.R., Tung J., Emerick R.S., Masiarz F.R., Chamberlain S.H.,
RA Vasavada A., Rosenberg S., Chakraborty S., Schopter L.M., Massey V.;
RT "Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion
RT from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived
RT enzyme.";
RL J. Biol. Chem. 265:3793-3802(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-32.
RX PubMed=2076553; DOI=10.1007/bf00327024;
RA Whittington H., Kerry-Williams S., Bidgood K., Dodsworth N., Peberdy J.,
RA Dobson M., Hinchliffe E., Ballance D.J.;
RT "Expression of the Aspergillus niger glucose oxidase gene in A. niger, A.
RT nidulans and Saccharomyces cerevisiae.";
RL Curr. Genet. 18:531-536(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=8421298; DOI=10.1006/jmbi.1993.1015;
RA Hecht H.-J., Kalisz H.M., Hendle J., Schmid R.D., Schomburg D.;
RT "Crystal structure of glucose oxidase from Aspergillus niger refined at
RT 2.3-A resolution.";
RL J. Mol. Biol. 229:153-172(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 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 molds 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 -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/GOP/";
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DR EMBL; X16061; CAA34197.1; -; Genomic_DNA.
DR EMBL; J05242; AAA32695.1; -; mRNA.
DR EMBL; X56443; CAA39826.1; -; Genomic_DNA.
DR PIR; A35459; A35459.
DR PDB; 1CF3; X-ray; 1.90 A; A=23-605.
DR PDB; 1GAL; X-ray; 2.30 A; A=23-605.
DR PDB; 3QVP; X-ray; 1.20 A; A=23-605.
DR PDB; 3QVR; X-ray; 1.30 A; A=23-605.
DR PDB; 5NIT; X-ray; 1.87 A; A=25-605.
DR PDB; 5NIW; X-ray; 1.80 A; A=25-605.
DR PDBsum; 1CF3; -.
DR PDBsum; 1GAL; -.
DR PDBsum; 3QVP; -.
DR PDBsum; 3QVR; -.
DR PDBsum; 5NIT; -.
DR PDBsum; 5NIW; -.
DR AlphaFoldDB; P13006; -.
DR PCDDB; P13006; -.
DR SMR; P13006; -.
DR STRING; 5061.CADANGAP00001413; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR CLAE; GOX3B_ASPNG; -.
DR ABCD; P13006; 1 sequenced antibody.
DR VEuPathDB; FungiDB:An01g14740; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1132679; -.
DR VEuPathDB; FungiDB:ATCC64974_11640; -.
DR VEuPathDB; FungiDB:M747DRAFT_316207; -.
DR eggNOG; KOG1238; Eukaryota.
DR BioCyc; MetaCyc:MON-17584; -.
DR BRENDA; 1.1.3.4; 518.
DR SABIO-RK; P13006; -.
DR EvolutionaryTrace; P13006; -.
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; Signal.
FT SIGNAL 1..22
FT /note="Or 48"
FT CHAIN 23..605
FT /note="Glucose oxidase"
FT /id="PRO_0000012338"
FT ACT_SITE 538
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 43..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 186..228
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3QVP"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3QVP"
FT TURN 90..95
FT /evidence="ECO:0007829|PDB:3QVP"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:3QVP"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:3QVP"
FT TURN 255..260
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 298..309
FT /evidence="ECO:0007829|PDB:3QVP"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3QVR"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3QVR"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 411..427
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 480..497
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 522..528
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:3QVP"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:1CF3"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:3QVP"
FT HELIX 583..603
FT /evidence="ECO:0007829|PDB:3QVP"
SQ SEQUENCE 605 AA; 65638 MW; 25243E5ED1D2773B CRC64;
MQTLLVSSLV VSLAAALPHY IRSNGIEASL LTDPKDVSGR TVDYIIAGGG LTGLTTAARL
TENPNISVLV IESGSYESDR GPIIEDLNAY GDIFGSSVDH AYETVELATN NQTALIRSGN
GLGGSTLVNG GTWTRPHKAQ VDSWETVFGN EGWNWDNVAA YSLQAERARA PNAKQIAAGH
YFNASCHGVN GTVHAGPRDT GDDYSPIVKA LMSAVEDRGV PTKKDFGCGD PHGVSMFPNT
LHEDQVRSDA AREWLLPNYQ RPNLQVLTGQ YVGKVLLSQN GTTPRAVGVE FGTHKGNTHN
VYAKHEVLLA AGSAVSPTIL EYSGIGMKSI LEPLGIDTVV DLPVGLNLQD QTTATVRSRI
TSAGAGQGQA AWFATFNETF GDYSEKAHEL LNTKLEQWAE EAVARGGFHN TTALLIQYEN
YRDWIVNHNV AYSELFLDTA GVASFDVWDL LPFTRGYVHI LDKDPYLHHF AYDPQYFLNE
LDLLGQAAAT QLARNISNSG AMQTYFAGET IPGDNLAYDA DLSAWTEYIP YHFRPNYHGV
GTCSMMPKEM GGVVDNAARV YGVQGLRVID GSIPPTQMSS HVMTVFYAMA LKISDAILED
YASMQ
