Q5G234 (P2OX_TRAPU) 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:	p2o

Organism

Trametes pubescens (White-rot fungus)

Taxonomic identifier

154538 [NCBI]

Taxonomic lineage

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

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 By similarity. Ref.1
Catalytic activity	D-glucose + O2 = 2-dehydro-D-glucose + H2O2.
Cofactor	Binds 1 FAD covalently per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Periplasm By similarity. Note: Hyphal periplasmic space By similarity.
Sequence similarities	Belongs to the GMC oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=133 mM for L-arabinose (at pH 6.5 and 30 degrees Celsius) Ref.1 KM=9.91 mM for D-galactose (at pH 6.5 and 30 degrees Celsius) KM=1.31 mM for D-glucose (at pH 6.5 and 30 degrees Celsius) KM=157 mM for melibiose (at pH 6.5 and 30 degrees Celsius) KM=123 mM for ribose (at pH 6.5 and 30 degrees Celsius) KM=75.4 mM for L-sorbose (at pH 6.5 and 30 degrees Celsius) KM=36.2 mM for D-xylose (at pH 6.5 and 30 degrees Celsius) Vmax=0.08 µmol/min/mg enzyme toward L-arabinose (at pH 6.5 and 30 degrees Celsius) Vmax=1.52 µmol/min/mg enzyme toward D-galactose (at pH 6.5 and 30 degrees Celsius) Vmax=9.32 µmol/min/mg enzyme toward D-glucose (at pH 6.5 and 30 degrees Celsius) Vmax=1.30 µmol/min/mg enzyme toward melibiose (at pH 6.5 and 30 degrees Celsius) Vmax=0.01 µmol/min/mg enzyme toward ribose (at pH 6.5 and 30 degrees Celsius) Vmax=12.50 µmol/min/mg enzyme toward L-sorbose (at pH 6.5 and 30 degrees Celsius) Vmax=4.02 µmol/min/mg enzyme toward D-xylose (at pH 6.5 and 30 degrees Celsius) pH dependence: Optimum pH is 5.5-6.5.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
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 – 38	10	By similarity		PRO_0000012354
	Chain	39 – 622	584	Pyranose 2-oxidase By similarity		PRO_0000012355
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

Sequences

	Sequence		Length	Mass (Da)
	Q5G234 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 48B91FB6304D3FC4	FASTA	622	69,214
	10 20 30 40 50 60 MSTSSSDPFY NFAKTSFKSA AAQKASATSL PPLPGPDQKV PGMDIKYDVV IVGSGPIGCT 70 80 90 100 110 120 YARELVEAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNK 130 140 150 160 170 180 LVVDTLSPTS WQASTFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR 190 200 210 220 230 240 PLLVKDDPDA DDAIWDQLYT KAESYFKTGT DQFNESIRHN LVLNKLAEEY KGQRTFQQIP 250 260 270 280 290 300 LAATRRNPTF VEWSSANTVF DLQNRPNIDA PEERFNLFPA VACERVMRNA SNTAIESLHI 310 320 330 340 350 360 RDLISGDRFA IQADVYVLTA GAVHNTQLLV NSGFGKLGRP DPANPPELLP FLGSYITEQS 370 380 390 400 410 420 LVFCQTVMST ELIDSVKSDM TIIGNPGELG YSVSYMPGAS TNKHPDWWNE KVQNHMMQHQ 430 440 450 460 470 480 EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK 490 500 510 520 530 540 EENKLWFSDK ITDAYNMPQP TFDFRFPAGR TSQEAEDMMT DMCVMSAKIG GFLPGSLPQF 550 560 570 580 590 600 MEPGLVLHLG GTHRMGFDEQ EDNCCVDTDS RVFGFNNLFL GGCGNIPTAY GANPTLTAMS 610 620 LAIKSCEYIK KNFTPSPFTP AQ

References

[1]

"Expression of the pyranose 2-oxidase from Trametes pubescens in Escherichia coli and characterization of the recombinant enzyme." Maresova H., Vecerek B., Hradska M., Libessart N., Becka S., Saniez M.-H., Kyslik P. J. Biotechnol. 120:387-395(2005) [PubMed: 16105703] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: CBS 696.94.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY863215 mRNA. Translation: AAW57304.1.
3D structure databases
ProteinModelPortal	Q5G234.
SMR	Q5G234. Positions 43-619.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR007867. GMC_OxRtase_C. IPR012814. Pyranose_ox. [Graphical view]
Pfam	PF05199. GMC_oxred_C. 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_TRAPU

Accession

Primary (citable) accession number: Q5G234

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	March 1, 2005
Last modified:	June 28, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program