P2OX_TRIMT
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 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;
DE Flags: Precursor;
GN Name=p2ox; Synonyms=p2o;
OS Tricholoma matsutake (Matsutake mushroom) (Tricholoma nauseosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; 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 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. Acts
CC also on D-xylose, L-sorbose, D-galactose and 1,5-anhydroglucitol, a
CC 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;
CC Evidence={ECO:0000269|PubMed:14730138};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:14730138};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.28 mM for D-glucose {ECO:0000269|PubMed:14730138};
CC KM=45.8 mM for D-xylose {ECO:0000269|PubMed:14730138};
CC KM=26.4 mM for L-sorbose {ECO:0000269|PubMed:14730138};
CC KM=45.0 mM for D-galactose {ECO:0000269|PubMed:14730138};
CC KM=10.7 mM for 1,5-anhydro-D-glucitol {ECO:0000269|PubMed:14730138};
CC KM=192 mM for trehalose {ECO:0000269|PubMed:14730138};
CC KM=329 mM for maltose {ECO:0000269|PubMed:14730138};
CC KM=295 mM for mannose {ECO:0000269|PubMed:14730138};
CC KM=174 mM for D-arabinose {ECO:0000269|PubMed:14730138};
CC Vmax=26.6 umol/min/mg enzyme with D-glucose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=13.4 umol/min/mg enzyme with D-xylose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=17.9 umol/min/mg enzyme with L-sorbose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=5.41 umol/min/mg enzyme with D-galactose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=18.4 umol/min/mg enzyme with 1,5-anhydro-D-glucitol as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=14.3 umol/min/mg enzyme with trehalose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=15.1 umol/min/mg enzyme with maltose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=6.02 umol/min/mg enzyme with mannose as substrate
CC {ECO:0000269|PubMed:14730138};
CC Vmax=1.87 umol/min/mg enzyme with D-arabinose as substrate
CC {ECO:0000269|PubMed:14730138};
CC pH dependence:
CC Optimum pH is 7.5-8.0. Active from pH 6 to 10. Stable from pH 5 to
CC 11. {ECO:0000269|PubMed:14730138};
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. {ECO:0000269|PubMed:14730138};
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB043883; BAC24805.1; -; mRNA.
DR AlphaFoldDB; Q8J2V8; -.
DR SMR; Q8J2V8; -.
DR BioCyc; MetaCyc:MON-14333; -.
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.
FT PROPEP 1..25
FT /evidence="ECO:0000269|PubMed:14730138"
FT /id="PRO_0000012358"
FT CHAIN 26..564
FT /note="Pyranose 2-oxidase"
FT /id="PRO_0000012359"
FT ACT_SITE 498
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 541
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="D -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="A -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="D -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="I -> M (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 496..497
FT /note="AQ -> VL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
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
