ID A0A0F0IG55_ASPPU Unreviewed; 580 AA.
AC A0A0F0IG55;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyranose 2-oxidase {ECO:0000256|ARBA:ARBA00016408};
DE EC=1.1.3.10 {ECO:0000256|ARBA:ARBA00013082};
DE AltName: Full=FAD-oxidoreductase {ECO:0000256|ARBA:ARBA00031159};
DE AltName: Full=Glucose 2-oxidase {ECO:0000256|ARBA:ARBA00030508};
DE AltName: Full=Pyranose:oxygen 2-oxidoreductase {ECO:0000256|ARBA:ARBA00031330};
GN ORFNames=P875_00127967 {ECO:0000313|EMBL:KJK66675.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66675.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK66675.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + O2 = 2-dehydro-D-glucose + H2O2;
CC Xref=Rhea:RHEA:10552, ChEBI:CHEBI:4167, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16609; EC=1.1.3.10;
CC Evidence={ECO:0000256|ARBA:ARBA00000827};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK66675.1}.
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DR EMBL; JZEE01000235; KJK66675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IG55; -.
DR STRING; 1403190.A0A0F0IG55; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050233; F:pyranose oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.1920.50; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR012814; P2OX.
DR NCBIfam; TIGR02462; pyranose_ox; 1.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT DOMAIN 443..570
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 580 AA; 65069 MW; 62D955B83FDA0D0F CRC64;
MVHTEYDALI VGSGPIGATY AKYLVEDGKK VLMVETGTQE SEIPGDHKKN AINFQKDIDA
FVHVIQGSLH HTSVPTNKSA VPTLAPVCWK ANGQIFNGQN PRQDPAVNLD ANGVARNVGG
MSTHWTCATP RQNKKEERSD IFTEKEWDRL YDEAEKLIGT RTDVLNDSIR QELVLRILND
EYGKRPAEPL PLAAKKKNDK TTFITWSSSS TIFDAMQHKE KFTLWPEHHC EKFVVEKTDN
GPQVTKAEIR NLATNELIPV KAKVFIACGG PILTPQLLFN SGFVPTKPHR DPRTQIPLED
DEEGIAPPPD TPEHLKLPAL GRYLTEQSMC FCQIVLKKKW VRAVAEKDYN PYQDDGVKRK
KWAKAKEGWN EKVQKHKKEF KEDPIPFPFD DMDPQVTLPL DSAHPWHTQI HRDAFSYGAA
PPAIDKRTIV DLRFFGKVEP DWNNYVTFES DIKDAYGMPQ PTFRYKLNED DRDQSHRMMK
DMEEAAGALG GYLPGSEPQF LAPGLALHVC GTTRAQKKEK ECDPDPKETS CCDENSKIWG
IPNLYVGGLN VIPGANGSNP TLTAMCFAIK SAKSILEGNP
//
