NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-57 AND 436-502, BIOPHYSICOCHEMICAL PROPERTIES, FAD-BINDING, AND TETRAMERIZATION.
DOI=10.1271/bbb.67.2598; PubMed=14730138 [NCBI, ExPASy, EBI, Israel, Japan]
Takakura Y., Kuwata S.;
"Purification, characterization, and molecular cloning of a pyranose oxidase from the fruit body of the basidiomycete, Tricholoma matsutake.";
Biosci. Biotechnol. Biochem. 67:2598-2607(2003).

Comments

FUNCTION: Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose. Acts also on D-xylose, L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.
CATALYTIC ACTIVITY: D-glucose + O₂ = 2-dehydro-D-glucose + H₂O₂.
COFACTOR: Binds 1 FAD covalently per subunit.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=1.28 mM for D-glucose;
	K_M=45.8 mM for D-xylose;
	K_M=26.4 mM for L-sorbose;
	K_M=45.0 mM for D-galactose;
	K_M=10.7 mM for 1,5-anhydro-D-glucitol;
	K_M=192 mM for trehalose;
	K_M=329 mM for maltose;
	K_M=295 mM for mannose;
	K_M=174 mM for D-arabinose;
	V_max=26.6 µmol/min/mg enzyme with D-glucose as substrate;
	V_max=13.4 µmol/min/mg enzyme with D-xylose as substrate;
	V_max=17.9 µmol/min/mg enzyme with L-sorbose as substrate;
	V_max=5.41 µmol/min/mg enzyme with D-galactose as substrate;
	V_max=18.4 µmol/min/mg enzyme with 1,5-anhydro-D-glucitol as substrate;
	V_max=14.3 µmol/min/mg enzyme with trehalose as substrate;
	V_max=15.1 µmol/min/mg enzyme with maltose as substrate;
	V_max=6.02 µmol/min/mg enzyme with mannose as substrate;
	V_max=1.87 µmol/min/mg enzyme with D-arabinose as substrate;
pH dependence:	Optimum pH is 7.5-8.0. Active from pH 6 to 10. Stable from pH 5 to 11;
Temperature dependence:	Optimum temperature is 50 degrees Celsius. Active from 30 to 65 degrees Celsius. Thermostable for 30 minutes up to 55 degrees Celsius;

SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the GMC oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB043883; BAC24805.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q8J2V8.

Ontologies

GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0050233;	Molecular function: pyranose oxidase activity (inferred from electronic annotation from InterPro).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000172; GMC_OxRdtase_N.
IPR012814; Pyranose_ox.
Graphical view of domain structure.

TIGRFAMs

TIGR02462; pyranose_ox; 1.

PROSITE

PS00623; GMC_OXRED_1; FALSE_NEG.
PS00624; GMC_OXRED_2; FALSE_NEG.

ProtoNet

Q8J2V8.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 25`	`25`		`PRO_0000012358`
`CHAIN`	`26 564`	`539`	`Pyranose 2-oxidase.`	`PRO_0000012359`
`ACT_SITE`	`498 498`		`By similarity.`
`ACT_SITE`	`541 541`		`By similarity.`
`BINDING`	`392 392`		`Substrate (By similarity).`
`BINDING`	`394 394`		`Substrate (By similarity).`
`MOD_RES`	`158 158`		`Tele-8alpha-FAD histidine (By similarity).`
`CONFLICT`	`26 26`		`D -> H (in Ref. 1; AA sequence).`
`CONFLICT`	`43 43`		`A -> S (in Ref. 1; AA sequence).`
`CONFLICT`	`437 437`		`D -> E (in Ref. 1; AA sequence).`
`CONFLICT`	`478 478`		`I -> M (in Ref. 1; AA sequence).`
`CONFLICT`	`496 497`		`AQ -> VL (in Ref. 1; AA sequence).`

Sequence information

Length: 564 AA [This is the length of the unprocessed precursor]

Molecular weight: 61942 Da [This is the MW of the unprocessed precursor]

CRC64: 134790030045FC1B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPIRLSKEKI NDLLQRSQGD LTSSQDEIVH YTDVFIAGSG PIACTYARHI IDNTSTTKVY 

        70         80         90        100        110        120 
MAEIGSQDNP VIGAHHRNSI KFQKDTDKFV NIINGALQPI SISPSDTYQP TLAVAAWAPP 

       130        140        150        160        170        180 
IDPAEGQLVI MGHNPNQEAG LNLPGSAVTR TVGGMATHWT CACPTPHDEE RVNNPVDKQE 

       190        200        210        220        230        240 
FDALLERAKT LLNVHSDQYD DSIRQIVVKE TLQQTLDASR GVTTLPLGVE RRTDNPIYVT 

       250        260        270        280        290        300 
WTGADTVLGD VPKSPRFVLV TETRVTKFIV SETNPTQVVA ALLRNLNTSN DELVVAQSFV 

       310        320        330        340        350        360 
IACGAVCTPQ ILWNSNIRPH ALGRYLSEQS MTFCQIVLKR SIVDSIATDP RFAAKVEAHK 

       370        380        390        400        410        420 
KKHPDDVLPI PFHEPEPQVM IPYTSDFPWH VQVHRYAFGD VGPKADPRVV VDLRFFGKSD 

       430        440        450        460        470        480 
IVEENRVTFG PNPKLRDWEA GVTDTYGMPQ PTFHVKRTNA DGDRDQRMMN DMTNVANILG 

       490        500        510        520        530        540 
GYLPGSYPQF MAPGLAQHIT GTTRIGTDDQ TSVADPTSKV HNFDNLWVGG NGCIPDATAC 

       550        560 
NPTRTSVAYA LKGAEAVVSY LGVS

Q8J2V8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools