ID   P2OX_TRAHI              Reviewed;         622 AA.
AC   P59097;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 1.
DT   03-AUG-2022, entry version 69.
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;
DE   Flags: Precursor;
GN   Name=P2OX;
OS   Trametes hirsuta (White-rot fungus) (Coriolus hirsutus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-62; 232-254; 405-412;
RP   486-491 AND 575-596, CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 2987;
RA   Christensen S., Lassen S.F., Schneider P.;
RT   "Nucleic acids encoding polypeptides having pyranose oxidase activity.";
RL   Patent number US6146865, 14-NOV-2000.
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). Plays an important
CC       role in lignin degradation of wood rot fungi by supplying the essential
CC       cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin
CC       peroxidase and manganese-dependent peroxidase. The preferred substrate
CC       is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate
CC       of a secondary metabolic pathway leading to the antibiotic
CC       cortalcerone. Acts also on D-xylose, together with D-glucose the major
CC       sugars derived from wood, on L-sorbose, D-galactose and 1,5-
CC       anhydroglucitol, a diagnostic marker of diabetes mellitus.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6. Active and stable from pH 3 to 9.
CC         {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 30-50 degrees Celsius. Active and thermostable
CC         for 30 minutes up to 55 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Hyphal periplasmic
CC       space. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   AlphaFoldDB; P59097; -.
DR   SMR; P59097; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR012814; P2OX.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02462; pyranose_ox; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Periplasm;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   PROPEP          29..37
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000012352"
FT   CHAIN           38..622
FT                   /note="Pyranose 2-oxidase"
FT                   /id="PRO_0000012353"
FT   ACT_SITE        546
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   ACT_SITE        591
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         167
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        60
FT                   /note="T -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243..244
FT                   /note="AT -> FS (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   622 AA;  69082 MW;  0B616C02014E7C5B CRC64;
     MSASSSDPFH SFAKTSFTSK AAKRATAHSL PPLPGPGDLP PGMNVEYDVA IVGSGPIGCT
     YARELVEAGF NVAMFEIGEI DSGLKIGSHK KNTVEYQKNI DKFVNVIQGQ LMPVSVPVNT
     MVVDTLSPAS WQASTFFVRN GANPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFEKLQR
     PLLVKNDSKA DDAEWDRLYK KAESYFKTGT TQFAESIRHN LVLKKLQEEY KGVRDFQQIP
     LAATRQSPTF VEWSSAHTVF DLENRPNKDA PKQRFNLFPA VACTNVRRDN ANSEIVGLDV
     RDLHGGKSIT IKAKVYILTA GAVHNAQLLA ASGFGQLGRP DPAKPLPSLL PYLGTHITEQ
     TLVFCQTVMS TELINSVTAD MTIVGKPGHP DYSVTYTPGN PNNKHPDWWN EKVKKHMMDH
     QEDPLPIPFE DPEPQVTTLF QATHPWHTQI HRDAFSYGAV QQSIDSRLIV DWRFFGRTEP
     KEENKLWFSD KITDAYNLRQ PTFDFRFPGG REAEDMMTDM CVMSAKIGGF LPGSYPQFME
     PGLVLHLGGT HRMGFDEKAD KCCVDTDSRV FGFKNLFLGG CGNIPTAYAA NPTLTAMSLA
     IKSCEYIKKN FEPSPNPVKH HN