GOX_TALFL
ID GOX_TALFL Reviewed; 605 AA.
AC Q92452;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Talaromyces flavus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=5095;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 32908;
RX PubMed=9371889; DOI=10.1007/s002940050290;
RA Murray F.R., Llewellyn D.J., Peacock W.J., Dennis E.S.;
RT "Isolation of the glucose oxidase gene from Talaromyces flavus and
RT characterisation of its role in the biocontrol of Verticillium dahliae.";
RL Curr. Genet. 32:367-375(1997).
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U56240; AAB09442.1; -; Genomic_DNA.
DR AlphaFoldDB; Q92452; -.
DR SMR; Q92452; -.
DR CLAE; GOX3A_TALFL; -.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..605
FT /note="Glucose oxidase"
FT /id="PRO_0000012339"
FT ACT_SITE 538
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 44..73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 605 AA; 65769 MW; 746F5F77FD1558D3 CRC64;
MVSVFLSTLL LAAATVQAYL PAQQIDVQSS LLSDPSKVAG KTYDYIIAGG GLTGLTVAAK
LTENPKIKVL VIEKGFYESN DGAIIEDPNA YGQIFGTTVD QNYLTVPLIN NRTNNIKAGK
GLGGSTLING DSWTRPDKVQ IDSWEKVFGM EGWNWDSMFE YMKKAEAARA PTAAQLAAGH
YFNATCHGTN GTVQSGARDN GQPWSPIMKA LMNTVSALGV PVQQDFLCGH PRGVSMIMNN
VDENQVRVDA ARAWLLPSYQ RPNLEILTGQ MVGKVLFKQT ASGPQAVGVN FGTNKAVNFD
VFAKHEVLLA AGSAISPLIL EYSGIGLKSV LDQANVTQLL DLPVGINMQD QTTTTVSSRA
SAAGAGQGQA VFFANFTETF GDYAPQAREL LNTKLDQWAE ETVARGGFHN VTALKVQYEN
YRNWLLDEDV AFAELFMDTE GKINFDLWDL IPFTRGSVHI LSSDPYLWQF ANDPKFFLNE
FDLLGQAAAS KLARDLTSQG AMKEYFAGET LPGYNLVENA TLSQWSDYVL QNFRPNWHAV
SSCSMMSREL GGVVDATAKV YGTQGLRVID GSIPPTQVSS HVMTIFYGMA LKVADAILDD
YAKSA
