Q6UG02 (P2OX_PHLGI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyranose 2-oxidase
Short name=P2Ox
Short name=POD
Short name=POx
Short name=PROD
Short name=Pyranose oxidase
EC=1.1.3.10

Alternative name(s):
FAD-oxidoreductase
Glucose 2-oxidase
Pyranose:oxygen 2-oxidoreductase

Gene names

Name:	p2ox
Synonyms:	poxB

Organism

Phlebiopsis gigantea (White-rot fungus) (Peniophora gigantea)

Taxonomic identifier

82310 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Phanerochaetaceae › Phlebiopsis

Protein attributes

Sequence length	622 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.
Catalytic activity	D-glucose + O2 = 2-dehydro-D-glucose + H2O2.
Cofactor	Binds 1 FAD covalently per subunit. Ref.2
Subunit structure	Homotetramer. Ref.2
Subcellular location	Periplasm By 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=0.65 mM for O2 Ref.1 Ref.2 KM=1.1 mM for D-glucose KM=11.3 mM for 2-deoxy-D-glucose KM=289 mM for methyl-beta-D-glucoside KM=29.4 mM for D-xylose KM=50 mM for L-sorbose KM=8.2 mM for D-galactose KM=55.7 mM for D-allose Vmax=10.4 µmol/min/mg enzyme with D-glucose as substrate Vmax=4.5 µmol/min/mg enzyme with 2-deoxy-D-glucose as substrate Vmax=2.9 µmol/min/mg enzyme with methyl-beta-D-glucoside as substrate Vmax=4.3 µmol/min/mg enzyme with D-xylose as substrate Vmax=7.9 µmol/min/mg enzyme with L-sorbose as substrate Vmax=0.5 µmol/min/mg enzyme with D-galactose as substrate Vmax=3.7 µmol/min/mg enzyme with D-allose as substrate pH dependence: Optimum pH is 4.5-6.0. Active from pH 4 to 7.5. Stable from pH 4 to 11. Temperature dependence: Optimum temperature is 44 degrees Celsius. Active from 30 to 55 degrees Celsius. Thermostable for 30 minutes up to 50 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
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	flavin adenine dinucleotide 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
	Signal peptide	1 – 28	28	By similarity
	Propeptide	29 – 37	9	By similarity		PRO_0000012350
	Chain	38 – 622	585	Pyranose 2-oxidase		PRO_0000012351
Sites
	Active site	546	1	By similarity
	Active site	591	1	By similarity
	Binding site	449	1	Substrate By similarity
	Binding site	451	1	Substrate By similarity
Amino acid modifications
	Modified residue	167	1	Tele-8alpha-FAD histidine Probable
Experimental info
	Mutagenesis	167	1	H → C: Decreases activity by 90%. Ref.1
	Mutagenesis	312	1	K → E in P2OxB2H; increases the catalytic efficiency 5.3-fold for D-glucose, 2-fold for methyl-beta-D-glucoside, 59.9-fold for D-xylose, 69-fold for L-sorbose and 4.8-fold for D-galactose; when associated with K-540. Ref.1
	Mutagenesis	540	1	E → K in P2OxB1; increases thermostability up to 70 degrees Celsius and enhances pH stability in alkaline solution. Increases the catalytic efficiency 3.1-fold for D-xylose and 7.3-fold for L-sorbose, mainly by lowering the Km values for these two substrates to 6.6 mM and 5.4 mM, respectively. In P2OxB2H; increases the catalytic efficiency 5.3-fold for D-glucose, 2-fold for methyl-beta-D-glucoside, 59.9-fold for D-xylose, 69-fold for L-sorbose and 4.8-fold for D-galactose; when associated with K-312. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6UG02 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 3F69FC03DC6BF134	FASTA	622	68,902
	10 20 30 40 50 60 MSASSSDPFH SFAKTSFTSK AAKRATAHSL PPLPGPGDLP PGMNVEYDVA IVGSGPIGST 70 80 90 100 110 120 YARELVEAGF NVAMFEIGEI DSGLKIGSHK KNTVEYQKNI DKFVNVIQGQ LMPVSVPVNT 130 140 150 160 170 180 MVVDTLSPAS WQASTFFVRN GANPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFEKLQR 190 200 210 220 230 240 PLLVKNDPVA DDAEWDRLYK KAESYFKTGT TQFAESIRHN LVLKKLQEEY KGVRDFQQIP 250 260 270 280 290 300 LAATRQSPTF VEWSSAHTVF DLENRPNKDA PKQRFNLFPA VACTSVRRND ANSEIIGLDV 310 320 330 340 350 360 RDLHGGKSIT IKAKVYILTA GAVHNAQLLA ASGFGQLGRP DPAKPLPSLL PYLGTHITEQ 370 380 390 400 410 420 TLVFCQTVMS TELINSVTAD MTIVGKPGDP DYSVTYTSGS PNNKHPDWWN EKVKKHMMDH 430 440 450 460 470 480 QEDPLPIPFE DPEPQVTTLF KASHPWHTQI HRDAFSYGAV QQSIDSRLIV DWRFFGRTEP 490 500 510 520 530 540 KEENKLWFSD KITDAYNLPQ PTFDFRFPGG REAEDMMTDM CVMSAKIGGF LPGSYPQFME 550 560 570 580 590 600 PGLVLHLGGT HRMGFDEKAD KCCVDTDSRV FGFKNLFLGG CGNIPTAYAA NPTLTAMSLA 610 620 IKSCEYIKKN FEPSPNPVKH HN

References

[1]

"Engineering of pyranose 2-oxidase from Peniophora gigantea towards improved thermostability and catalytic efficiency." Bastian S., Rekowski M.J., Witte K., Heckmann-Pohl D.M., Giffhorn F. Appl. Microbiol. Biotechnol. 67:654-663(2005) [PubMed: 15660220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-52, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-167; LYS-312 AND GLU-540. Strain: DSM 13218.

[2]

"Purification and characterization of a pyranose oxidase from the basidiomycete Peniophora gigantea and chemical analyses of its reaction products." Danneel H.-J., Roessner E., Zeeck A., Giffhorn F. Eur. J. Biochem. 214:795-802(1993) [PubMed: 8319689] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TETRAMERIZATION, FAD-BINDING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY370876 mRNA. Translation: AAQ72486.1.
3D structure databases
ProteinModelPortal	Q6UG02.
SMR	Q6UG02. Positions 46-615.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000172. GMC_OxRdtase_N. IPR007867. GMC_OxRtase_C. IPR012814. Pyranose_ox. [Graphical view]
Pfam	PF05199. GMC_oxred_C. 1 hit. PF00732. GMC_oxred_N. 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_PHLGI

Accession

Primary (citable) accession number: Q6UG02

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	June 28, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program