Reviewed, UniProtKB/Swiss-Prot Q6QWR1 (P2OX_PHACH)

Names and origin

Protein names

Recommended name:
    Pyranose 2-oxidase
      Short name=P2Ox
      Short name=P2O
      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
Synonyms:	pox

Organism

Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)

Taxonomic identifier

5306 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length	621 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 O2 to H2O2. Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H2O2 for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. 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. Ref.3 Ref.5
Catalytic activity	D-glucose + O2 = 2-dehydro-D-glucose + H2O2.
Cofactor	Binds 1 FAD covalently per subunit. Ref.2
Enzyme regulation	Inhibited by HgCl2.
Subunit structure	Homotetramer. Ref.2
Subcellular location	Periplasm. Note: Hyphal periplasmic space. Ref.4
Developmental stage	During autolysis, associated with extracellular slime surrounding lysed hyphae. Ref.4
Induction	Induced by carbon starvation. Ref.4 Ref.1
Post-translational modification	Not glycosylated.
Sequence similarities	Belongs to the GMC oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=83.2 µM for O2 KM=1.43 mM for D-glucose KM=1.53 mM for alpha-D-glucose KM=0.97 mM for beta-D-glucose KM=55 mM for 2-deoxy-D-glucose KM=25 mM for D-xylose KM=108 mM for L-sorbose Vmax=26.64 µM/min/mg enzyme towards O2 pH dependence: Optimum pH is 8.0-8.5. Active from pH 4.5 to 10. Stable from pH 4 to 11. Temperature dependence: Optimum temperature is 55 degrees Celsius. Thermostable for 2 hours up to 70 degrees Celsius.

Ontologies

Keywords
Cellular component	Periplasm
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-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro pyranose oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 9	9			PRO_0000012348
	Chain	10 – 621	612	Pyranose 2-oxidase		PRO_0000012349
Sites
	Active site	553	1	By similarity
	Active site	596	1	By similarity
	Binding site	454	1	Substrate By similarity
	Binding site	456	1	Substrate By similarity
Amino acid modifications
	Modified residue	158	1	Tele-8alpha-FAD histidine By similarity
Experimental info
	Sequence conflict	78	1	H → S AA sequence Ref.2
	Sequence conflict	80	1	K → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6QWR1-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 08A1C1264D824A4C	FASTA	621	69,298
	10 20 30 40 50 60 MFLDTTPFRA DEPYDVFIAG SGPIGATFAK LCVDANLRVC MVEIGAADSF TSKPMKGDPN 70 80 90 100 110 120 APRSVQFGPG QVPIPGYHKK NEIEYQKDID RFVNVIKGAL STCSIPTSNN HIATLDPSVV 130 140 150 160 170 180 SNSLDKPFIS LGKNPAQNPF VNLGAEAVTR GVGGMSTHWT CATPEFFAPA DFNAPHRERP 190 200 210 220 230 240 KLSTDAAEDA RIWKDLYAQA KEIIGTSTTE FDHSIRHNLV LRKYNDIFQK ENVIREFSPL 250 260 270 280 290 300 PLACHRLTDP DYVEWHATDR ILEELFTDPV KRGRFTLLTN HRCTKLVFKH YRPGEENEVD 310 320 330 340 350 360 YALVEDLLPH MQNPGNPASV KKIYARSYVV ACGAVATAQV LANSHIPPDD VVIPFPGGEK 370 380 390 400 410 420 GSGGGERDAT IPTPLMPMLG KYITEQPMTF CQVVLDSSLM EVVRNPPWPG LDWWKEKVAR 430 440 450 460 470 480 HVEAFPNDPI PIPFRDPEPQ VTIKFTEEHP WHVQIHRDAF SYGAVAENMD TRVIVDYRFF 490 500 510 520 530 540 GYTEPQEANE LVFQQHYRDA YDMPQPTFKF TMSQDDRARA RRMMDDMCNI ALKIGGYLPG 550 560 570 580 590 600 SEPQFMTPGL ALHLAGTTRC GLDTQKTVGN THCKVHNFNN LYVGGNGVIE TGFAANPTLT 610 620 SICYAIRASN DIIAKFGRHR G

References

[1]	"Isolation and purification of pyranose 2-oxidase from Phanerochaete chrysosporium and characterization of gene structure and regulation." de Koker T.H., Mozuch M.D., Cullen D., Gaskell J., Kersten P.J. Appl. Environ. Microbiol. 70:5794-5800(2004) [PubMed: 15466516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-30; 66-96; 98-150; 182-191; 202-216; 223-229; 236-272; 275-282; 421-444; 458-472 AND 479-517, INDUCTION. Strain: ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767.
[2]	"Pyranose 2-oxidase from Phanerochaete chrysosporium -- further biochemical characterisation." Artolozaga M.J., Kubatova E., Volc J., Kalisz H.M. Appl. Microbiol. Biotechnol. 47:508-514(1997) [PubMed: 9210340] [Abstract] Cited for: PROTEIN SEQUENCE OF 66-96 AND 366-388, BIOPHYSICOCHEMICAL PROPERTIES, FAD-BINDING, TETRAMERIZATION.
[3]	"Pyranose oxidase and pyranosone dehydratase: enzymes responsible for conversion of D-glucose to cortalcerone by the basidiomycete Phanerochaete chrysosporium." Volc J., Kubatova E., Sedmera P., Daniel G., Gabriel J. Arch. Microbiol. 156:297-301(1991) Cited for: FUNCTION.
[4]	"Ultrastructural and immunocytochemical studies on the H(2)O(2)-producing enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid culture conditions." Daniel G., Volc J., Kubatova E., Nilsson T. Appl. Environ. Microbiol. 58:3667-3676(1992) [PubMed: 16348809] [Abstract] Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION.
[5]	"Only C-2 specific glucose oxidase activity is expressed in ligninolytic cultures of the white rot fungus Phanerochaete chrysosporium." Volc J., Kubatova E., Daniel G., Prikrylova V. Arch. Microbiol. 165:421-424(1996) [PubMed: 8661938] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY522922 mRNA. Translation: AAS93628.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.3.10. 16698.
Family and domain databases
InterPro	IPR000172. GMC_OxRdtase_N. IPR012814. Pyranose_ox. [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_PHACH

Accession

Primary (citable) accession number: Q6QWR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)