Reviewed, UniProtKB/Swiss-Prot P79076 (P2OX_TRAVE)

Names and origin

Protein names

Recommended name:
    Pyranose 2-oxidase
      Short name=P2Ox
      Short name=Pyranose oxidase
      Short name=PROD
      Short name=POD
      Short name=POx
    EC=1.1.3.10
Alternative name(s):
    Pyranose:oxygen 2-oxidoreductase
    Glucose 2-oxidase
    FAD-oxidoreductase

Gene names

Name:

P2OX

Organism

Trametes versicolor (White-rot fungus) (Coriolus versicolor)

Taxonomic identifier

5325 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Trametes

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 + O(2) = 2-dehydro-D-glucose + H(2)O(2).
Cofactor	Binds 1 FAD covalently per subunit.
Subunit structure	Homotetramer.
Subcellular location	PeriplasmBy similarity. Note= Hyphal periplasmic space By similarity.
Post-translational modification	Not glycosylated.
Sequence similarities	Belongs to the GMC oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=1.4 mM for D-glucose KM=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.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro pyranose oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Probable
	Propeptide	28 – 38	11			PRO_0000012356
	Chain	39 – 623	585	Pyranose 2-oxidase		PRO_0000012357
Sites
	Active site	548	1	By similarity
	Active site	593	1	By similarity
	Binding site	448	1	Substrate By similarity
	Binding site	450	1	Substrate By similarity
Amino acid modifications
	Modified residue	167	1	Tele-8alpha-FAD histidine By similarity
Experimental info
	Mutagenesis	542	1	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

Sequences

	Sequence		Length	Mass (Da)
	P79076-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 5D3FC81B35FA5B54	FASTA	623	69,495
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	D73369 mRNA. Translation: BAA11119.1.
3D structure databases
SMR	P79076. Positions 43-619.
ModBase	Search...
Family and domain databases
InterPro	IPR006076. FAD-dep_OxRdtase. IPR000172. GMC_OxRdtase_N. IPR012814. Pyranose_ox. [Graphical view]
Pfam	PF01266. DAO. 1 hit. [Graphical view]
TIGRFAMs	TIGR02462. pyranose_ox. 1 hit.
PROSITE	PS00623. GMC_OXRED_1. False negative. PS00624. GMC_OXRED_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P2OX_TRAVE

Accession

Primary (citable) accession number: P79076

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	May 1, 1997
Last modified:	November 25, 2008
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)