ID   P2OX_LYOSH              Reviewed;         618 AA.
AC   Q75ZP8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Pyranose 2-oxidase;
DE            Short=P2Ox;
DE            Short=POD;
DE            Short=POx;
DE            Short=PROD;
DE            Short=Pyranose oxidase;
DE            EC=1.1.3.10;
DE   AltName: Full=FAD-oxidoreductase;
DE   AltName: Full=Glucose 2-oxidase;
DE   AltName: Full=Pyranose:oxygen 2-oxidoreductase;
GN   Name=p2ox; Synonyms=lsp2o;
OS   Lyophyllum shimeji (Hon-shimeji) (Tricholoma shimeji).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Lyophyllaceae; Lyophyllum.
OX   NCBI_TaxID=47721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Takakura Y., Tsutsumi F., Inoue Y., Kuwata S.;
RT   "Identification and cloning of a novel pyranose oxidase with high catalytic
RT   activity from Lyophyllum shimeji and its expression in Escherichia coli.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of various aldopyranoses and
CC       disaccharides on carbon-2 to the corresponding 2-keto sugars
CC       concomitant with the reduction of O(2) to H(2)O(2). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD covalently per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AB119106; BAD12079.1; -; mRNA.
DR   AlphaFoldDB; Q75ZP8; -.
DR   SMR; Q75ZP8; -.
DR   CAZy; AA3; Auxiliary Activities 3.
DR   PRIDE; Q75ZP8; -.
DR   BRENDA; 1.1.3.10; 12323.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050233; F:pyranose oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR012814; P2OX.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02462; pyranose_ox; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..618
FT                   /note="Pyranose 2-oxidase"
FT                   /id="PRO_0000205613"
FT   ACT_SITE        540
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   ACT_SITE        583
FT                   /evidence="ECO:0000250"
FT   BINDING         441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         170
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   618 AA;  68488 MW;  255B99DF266BC541 CRC64;
     MSLSTEQMLR DYPRSMQING QIPKNAIHET YGNDGVDVFI AGSGPIGATY AKLCVEAGLR
     VVMVEIGAAD SFYAVNAEEG TAVPYVPGYH KKNEIEFQKD IDRFVNVIKG ALQQVSVPVR
     NQNVPTLDPG AWSAPPGSSA ISNGKNPHQR EFENLSAEAV TRGVGGMSTH WTCSTPRIHP
     PMESLPGIGR PKLSNDPAED DKEWNELYSE AERLIGTSTK EFDESIRHTL VLRSLQDAYK
     DRQRIFRPLP LACHRLKNAP EYVEWHSAEN LFHSIYNDDK QKKLFTLLTN HRCTRLALTG
     GYEKKIGAAE VRNLLATRNP SSQLDSYIMA KVYVLASGAI GNPQILYNSG FSGLQVTPRN
     DSLIPNLGRY ITEQPMAFCQ IVLRQEFVDS VRDDPYGLPW WKEAVAQHIA KNPTDALPIP
     FRDPEPQVTT PFTEEHPWHT QIHRDAFSYG AVGPEVDSRV IVDLRWFGAT DPEANNLLVF
     QNDVQDGYSM PQPTFRYRPS TASNVRARKM MADMCEVASN LGGYLPTSPP QFMDPGLALH
     LAGTTRIGFD KATTVADNNS LVWDFANLYV AGNGTIRTGF GENPTLTSMC HAIKSARSII
     NTLKGGTDGK NTGEHRNL