Reviewed, UniProtKB/Swiss-Prot P59097 (P2OX_TRAHI)

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 hirsuta (White-rot fungus) (Coriolus hirsutus)

Taxonomic identifier

5327 [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 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, 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 + O(2) = 2-dehydro-D-glucose + H(2)O(2).
Cofactor	Binds 1 FAD covalently per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	PeriplasmBy similarity. Note= Hyphal periplasmic space By similarity.
Sequence similarities	Belongs to the GMC oxidoreductase family.
Biophysicochemical properties	pH dependence: Optimum pH is 6. Active and stable from pH 3 to 9. Temperature dependence: Optimum temperature is 30-50 degrees Celsius. Active and 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 – 28	28	By similarity
	Propeptide	29 – 37	9			PRO_0000012352
	Chain	38 – 622	585	Pyranose 2-oxidase		PRO_0000012353
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 By similarity
Experimental info
	Sequence conflict	60	1	T → S AA sequence Ref.1
	Sequence conflict	243 – 244	2	AT → FS AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P59097-1 [UniParc]. Last modified November 15, 2002. Version 1. Checksum: 0B616C02014E7C5B	FASTA	622	69,082
	10 20 30 40 50 60 MSASSSDPFH SFAKTSFTSK AAKRATAHSL PPLPGPGDLP PGMNVEYDVA IVGSGPIGCT 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 PLLVKNDSKA DDAEWDRLYK KAESYFKTGT TQFAESIRHN LVLKKLQEEY KGVRDFQQIP 250 260 270 280 290 300 LAATRQSPTF VEWSSAHTVF DLENRPNKDA PKQRFNLFPA VACTNVRRDN ANSEIVGLDV 310 320 330 340 350 360 RDLHGGKSIT IKAKVYILTA GAVHNAQLLA ASGFGQLGRP DPAKPLPSLL PYLGTHITEQ 370 380 390 400 410 420 TLVFCQTVMS TELINSVTAD MTIVGKPGHP DYSVTYTPGN PNNKHPDWWN EKVKKHMMDH 430 440 450 460 470 480 QEDPLPIPFE DPEPQVTTLF QATHPWHTQI HRDAFSYGAV QQSIDSRLIV DWRFFGRTEP 490 500 510 520 530 540 KEENKLWFSD KITDAYNLRQ PTFDFRFPGG REAEDMMTDM CVMSAKIGGF LPGSYPQFME 550 560 570 580 590 600 PGLVLHLGGT HRMGFDEKAD KCCVDTDSRV FGFKNLFLGG CGNIPTAYAA NPTLTAMSLA 610 620 IKSCEYIKKN FEPSPNPVKH HN

References

[1]

"Nucleic acids encoding polypeptides having pyranose oxidase activity." Christensen S., Lassen S.F., Schneider P. Patent number US6146865, 14-NOV-2000 Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-62; 232-254; 405-412; 486-491 AND 575-596, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: DSM 2987.

Cross-references

3D structure databases
SMR	P59097. Positions 43-615.
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. 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_TRAHI

Accession

Primary (citable) accession number: P59097

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 15, 2002
Last modified:	November 25, 2008
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)