ID   P2OX_TRIMT              Reviewed;         564 AA.
AC   Q8J2V8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Pyranose 2-oxidase;
DE            Short=P2Ox;
DE            Short=Pyranose oxidase;
DE            Short=PROD;
DE            Short=POD;
DE            Short=POx;
DE            EC=1.1.3.10;
DE   AltName: Full=Pyranose:oxygen 2-oxidoreductase;
DE   AltName: Full=Glucose 2-oxidase;
DE   AltName: Full=FAD-oxidoreductase;
DE   Flags: Precursor;
GN   Name=p2ox; Synonyms=p2o;
OS   Tricholoma matsutake (Matsutake mushroom) (Tricholoma nauseosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Homobasidiomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
OC   Tricholoma.
OX   NCBI_TaxID=40145;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-57 AND 436-502,
RP   BIOPHYSICOCHEMICAL PROPERTIES, FAD-BINDING, AND TETRAMERIZATION.
RX   PubMed=14730138; DOI=10.1271/bbb.67.2598;
RA   Takakura Y., Kuwata S.;
RT   "Purification, characterization, and molecular cloning of a pyranose
RT   oxidase from the fruit body of the basidiomycete, Tricholoma
RT   matsutake.";
RL   Biosci. Biotechnol. Biochem. 67:2598-2607(2003).
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). The preferred
CC       substrate is D-glucose which is converted to 2-dehydro-D-glucose.
CC       Acts also on D-xylose, L-sorbose, D-galactose and 1,5-
CC       anhydroglucitol, a diagnostic marker of diabetes mellitus.
CC   -!- CATALYTIC ACTIVITY: D-glucose + O(2) = 2-dehydro-D-glucose +
CC       H(2)O(2).
CC   -!- COFACTOR: Binds 1 FAD covalently per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.28 mM for D-glucose;
CC         KM=45.8 mM for D-xylose;
CC         KM=26.4 mM for L-sorbose;
CC         KM=45.0 mM for D-galactose;
CC         KM=10.7 mM for 1,5-anhydro-D-glucitol;
CC         KM=192 mM for trehalose;
CC         KM=329 mM for maltose;
CC         KM=295 mM for mannose;
CC         KM=174 mM for D-arabinose;
CC         Vmax=26.6 umol/min/mg enzyme with D-glucose as substrate;
CC         Vmax=13.4 umol/min/mg enzyme with D-xylose as substrate;
CC         Vmax=17.9 umol/min/mg enzyme with L-sorbose as substrate;
CC         Vmax=5.41 umol/min/mg enzyme with D-galactose as substrate;
CC         Vmax=18.4 umol/min/mg enzyme with 1,5-anhydro-D-glucitol as
CC         substrate;
CC         Vmax=14.3 umol/min/mg enzyme with trehalose as substrate;
CC         Vmax=15.1 umol/min/mg enzyme with maltose as substrate;
CC         Vmax=6.02 umol/min/mg enzyme with mannose as substrate;
CC         Vmax=1.87 umol/min/mg enzyme with D-arabinose as substrate;
CC       pH dependence:
CC         Optimum pH is 7.5-8.0. Active from pH 6 to 10. Stable from pH 5
CC         to 11;
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Active from 30 to 65
CC         degrees Celsius. Thermostable for 30 minutes up to 55 degrees
CC         Celsius;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
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DR   EMBL; AB043883; BAC24805.1; -; mRNA.
DR   BRENDA; 1.1.3.10; 276073.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050233; F:pyranose oxidase activity; IEA:EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR012814; Pyranose_ox.
DR   TIGRFAMs; TIGR02462; pyranose_ox; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; FALSE_NEG.
DR   PROSITE; PS00624; GMC_OXRED_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT   PROPEP        1     25
FT                                /FTId=PRO_0000012358.
FT   CHAIN        26    564       Pyranose 2-oxidase.
FT                                /FTId=PRO_0000012359.
FT   ACT_SITE    498    498       By similarity.
FT   ACT_SITE    541    541       By similarity.
FT   BINDING     392    392       Substrate (By similarity).
FT   BINDING     394    394       Substrate (By similarity).
FT   MOD_RES     158    158       Tele-8alpha-FAD histidine (By
FT                                similarity).
FT   CONFLICT     26     26       D -> H (in Ref. 1; AA sequence).
FT   CONFLICT     43     43       A -> S (in Ref. 1; AA sequence).
FT   CONFLICT    437    437       D -> E (in Ref. 1; AA sequence).
FT   CONFLICT    478    478       I -> M (in Ref. 1; AA sequence).
FT   CONFLICT    496    497       AQ -> VL (in Ref. 1; AA sequence).
SQ   SEQUENCE   564 AA;  61942 MW;  134790030045FC1B CRC64;
     MPIRLSKEKI NDLLQRSQGD LTSSQDEIVH YTDVFIAGSG PIACTYARHI IDNTSTTKVY
     MAEIGSQDNP VIGAHHRNSI KFQKDTDKFV NIINGALQPI SISPSDTYQP TLAVAAWAPP
     IDPAEGQLVI MGHNPNQEAG LNLPGSAVTR TVGGMATHWT CACPTPHDEE RVNNPVDKQE
     FDALLERAKT LLNVHSDQYD DSIRQIVVKE TLQQTLDASR GVTTLPLGVE RRTDNPIYVT
     WTGADTVLGD VPKSPRFVLV TETRVTKFIV SETNPTQVVA ALLRNLNTSN DELVVAQSFV
     IACGAVCTPQ ILWNSNIRPH ALGRYLSEQS MTFCQIVLKR SIVDSIATDP RFAAKVEAHK
     KKHPDDVLPI PFHEPEPQVM IPYTSDFPWH VQVHRYAFGD VGPKADPRVV VDLRFFGKSD
     IVEENRVTFG PNPKLRDWEA GVTDTYGMPQ PTFHVKRTNA DGDRDQRMMN DMTNVANILG
     GYLPGSYPQF MAPGLAQHIT GTTRIGTDDQ TSVADPTSKV HNFDNLWVGG NGCIPDATAC
     NPTRTSVAYA LKGAEAVVSY LGVS
//