[1]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-63; 92-98; 186-207; 215-225; 378-411; 491-513 AND 611-621, CHARACTERIZATION, AND TETRAMERIZATION. STRAIN=ATCC 62976 / FES 1030 / IAM 13013 / IFO 30340 / Ps-4a; TISSUE=Mycelium; DOI=10.1016/S0168-1656(96)01618-5; PubMed=9025322 [NCBI, ExPASy, EBI, Israel, Japan] Nishimura I., Okada K., Koyama Y.; "Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor in Escherichia coli."; J. Biotechnol. 52:11-20(1996).
[2]	FAD-BINDING. AGRICOLA=IND85055664 Machida Y., Nakanishi T.; "Purification and properties of pyranose oxidase from Coriolus versicolor."; Agric. Biol. Chem. 48:2463-2470(1984).
[3]	FUNCTION. PubMed=16349330 [NCBI, ExPASy, EBI, Israel, Japan] Daniel G., Volc J., Kubatova E.; "Pyranose oxidase, a major source of H(2)O(2) during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida."; Appl. Environ. Microbiol. 60:2524-2532(1994).
[4]	BIOPHYSICOCHEMICAL PROPERTIES, TETRAMERIZATION, AND MUTAGENESIS OF GLU-542. DOI=10.1023/A:1005460028591 Masuda-Nishimura I., Minamihara T., Koyama Y.; "Improvement in thermal stability and reactivity of pyranose oxidase from Coriolus versicolor by random mutagenesis."; Biotechnol. Lett. 21:203-207(1999).

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). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on 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=1.4 mM for D-glucose;
Kinetic parameters:	K_M=35.3 mM for 1,5-anhydro-D-glucitol;
pH dependence:	Optimum pH is about 6.5. Active from pH 5 to 9. Stable from pH 3 to 11;
Temperature dependence:	Optimum temperature is about 50 degrees Celsius. Active from 30 to 65 degrees Celsius. Thermostable for 30 minutes up to 55 degrees Celsius;

SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Periplasm (By similarity). Note=Hyphal periplasmic space (By similarity).
PTM: Not glycosylated.
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

D73369; BAA11119.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

P79076; 43-619.

ModBase

P79076.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
IPR000172; GMC_OxRdtase_N.
IPR012814; Pyranose_ox.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02462; pyranose_ox; 1.

PROSITE

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

Other

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

Keywords

Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 27`	`27`	`Probable.`
`PROPEP`	`28 38`	`11`		`PRO_0000012356`
`CHAIN`	`39 623`	`585`	`Pyranose 2-oxidase.`	`PRO_0000012357`
`ACT_SITE`	`548 548`		`By similarity.`
`ACT_SITE`	`593 593`		`By similarity.`
`BINDING`	`448 448`		`Substrate (By similarity).`
`BINDING`	`450 450`		`Substrate (By similarity).`
`MOD_RES`	`167 167`		`Tele-8alpha-FAD histidine (By similarity).`
`MUTAGEN`	`542 542`		`E->K: Increases thermostability up to 65 degrees Celsius and enhances pH stability in alkaline solution. Increases the catalytic efficiency 2-fold for D-glucose and 3-fold for 1,5-anhydro-D-glucitol, mainly by lowering the Km values for these two substrates to 0.74 mM and 14.3 mM, respectively.`

Sequence information

Length: 623 AA [This is the length of the unprocessed precursor]

Molecular weight: 69495 Da [This is the MW of the unprocessed precursor]

CRC64: 5D3FC81B35FA5B54 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTSSSDPFF NFTKSSFRSA AAQKASATSL PPLPGPDKKV PGMDIKYDVV IVGSGPIGCT 

        70         80         90        100        110        120 
YARELVEAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNT 

       130        140        150        160        170        180 
LVIDTLSPTS WQASSFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR 

       190        200        210        220        230        240 
PLLVKDDQDA DDAEWDRLYT KAESYFKTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP 

       250        260        270        280        290        300 
LAATRRSPTF VEWSSANTVF DLQNRPNTDA PNERFNLFPA VACERVVRNT SNSEIESLHI 

       310        320        330        340        350        360 
HDLISGDRFE IKADVFVLTA GAVHNAQLLV NSGFGQLGRP DPANPPQLLP SLGSYITEQS 

       370        380        390        400        410        420 
LVFCQTVMST ELIDSVKSDM IIRGNPGDLG YSVTYTPGAE TNKHPDWWNE KVKNHMMQHQ 

       430        440        450        460        470        480 
EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK 

       490        500        510        520        530        540 
EENKLWFSDK ITDTYNMPQP TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF 

       550        560        570        580        590        600 
MEPGLVLHLG GTHRMGFDEQ EDKCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS 

       610        620 
LAIKSCEYIK NNFTPSPFTD QAE

P79076 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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