[1]	NUCLEOTIDE SEQUENCE [MRNA]. Heckmann-Pohl D.M., Bastian S., Rekowski M.J., Giffhorn F.; "Pyranose oxidase of the white-rot fungus Peniophora sp. strain SG: Cloning and characterization of the gene, heterologous expression in Escherichia coli, and properties of the recombinant enzyme."; Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[2]	X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), TETRAMERIZATION, COFACTOR, AND FAD-BINDING SITE. DOI=10.1021/bi048609q; PubMed=15362852 [NCBI, ExPASy, EBI, Israel, Japan] Bannwarth M., Bastian S., Heckmann-Pohl D.M., Giffhorn F., Schulz G.E.; "Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp."; Biochemistry 43:11683-11690(2004).

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 (By similarity).
CATALYTIC ACTIVITY: D-glucose + O₂ = 2-dehydro-D-glucose + H₂O₂.
COFACTOR: Binds 1 FAD covalently per subunit.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Periplasm (By similarity). Note=Hyphal periplasmic space (By similarity).
SIMILARITY: Belongs to the GMC oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF535193; AAO13382.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1TZL; X-ray; 2.35 A; A/B/C/D/E/F/G/H=2-623.	[ExPASy / RCSB / EBI]
2F5V; X-ray; 1.41 A; A=29-623.	[ExPASy / RCSB / EBI]
2F6C; X-ray; 1.84 A; A=29-623.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1TZL; -.
2F5V; -.
2F6C; -.

ModBase

Q8J136.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0050233;	Molecular function: pyranose oxidase activity (inferred from electronic annotation from InterPro).
GO:0006006;	Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
IPR000172; GMC_OxRdtase_N.
IPR012814; Pyranose_ox.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02462; pyranose_ox; 1.

PROSITE

PS00623; GMC_OXRED_1; FALSE_NEG.
PS00624; GMC_OXRED_2; FALSE_NEG.

Other

ProtoNet

Q8J136.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; FAD; Flavoprotein; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 28`	`28`	`Potential.`
`PROPEP`	`29 38`	`10`	`By similarity.`	`PRO_0000012346`
`CHAIN`	`39 623`	`585`	`Pyranose 2-oxidase.`	`PRO_0000012347`
`ACT_SITE`	`548 548`
`ACT_SITE`	`593 593`
`BINDING`	`448 448`		`Substrate.`
`BINDING`	`450 450`		`Substrate.`
`MOD_RES`	`167 167`		`Tele-8alpha-FAD histidine.`
`STRAND`	`45 52`	`8`
`HELIX`	`56 67`	`12`
`STRAND`	`71 75`	`5`
`STRAND`	`82 85`	`4`
`HELIX`	`94 98`	`5`
`HELIX`	`100 102`	`3`
`HELIX`	`103 109`	`7`
`STRAND`	`112 114`	`3`
`HELIX`	`163 166`	`4`
`HELIX`	`177 179`	`3`
`STRAND`	`183 186`	`4`
`HELIX`	`188 206`	`19`
`STRAND`	`208 210`	`3`
`TURN`	`212 215`	`4`
`HELIX`	`217 229`	`13`
`TURN`	`230 232`	`3`
`STRAND`	`241 247`	`7`
`STRAND`	`250 253`	`4`
`HELIX`	`256 259`	`4`
`STRAND`	`265 267`	`3`
`STRAND`	`270 278`	`9`
`STRAND`	`280 288`	`9`
`STRAND`	`295 302`	`8`
`TURN`	`303 305`	`3`
`STRAND`	`308 318`	`11`
`HELIX`	`322 331`	`10`
`STRAND`	`347 349`	`3`
`TURN`	`350 353`	`4`
`STRAND`	`361 369`	`9`
`HELIX`	`370 376`	`7`
`TURN`	`377 379`	`3`
`STRAND`	`381 384`	`4`
`STRAND`	`392 394`	`3`
`HELIX`	`406 418`	`13`
`STRAND`	`434 436`	`3`
`STRAND`	`445 450`	`6`
`HELIX`	`465 467`	`3`
`STRAND`	`468 475`	`8`
`STRAND`	`484 492`	`9`
`STRAND`	`496 503`	`8`
`HELIX`	`510 526`	`17`
`TURN`	`527 529`	`3`
`STRAND`	`530 532`	`3`
`STRAND`	`538 540`	`3`
`TURN`	`543 546`	`4`
`TURN`	`559 563`	`5`
`STRAND`	`576 580`	`5`
`HELIX`	`583 585`	`3`
`HELIX`	`595 612`	`18`

Sequence information

Length: 623 AA [This is the length of the unprocessed precursor]

Molecular weight: 69342 Da [This is the MW of the unprocessed precursor]

CRC64: 4B7DB64A387F43D5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTSSSDPFF NFAKSSFRSA AAQKASASSL PPLPGPDKKV PGMDIKYDVV IVGSGPIGCT 

        70         80         90        100        110        120 
YARELVGAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNT 

       130        140        150        160        170        180 
LVVDTLSPTS WQASTFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR 

       190        200        210        220        230        240 
PLLVKDDADA DDAEWDRLYT KAESYFQTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP 

       250        260        270        280        290        300 
LAATRRSPTF VEWSSANTVF DLQNRPNTDA PEERFNLFPA VACERVVRNA LNSEIESLHI 

       310        320        330        340        350        360 
HDLISGDRFE IKADVYVLTA GAVHNTQLLV NSGFGQLGRP NPTNPPELLP SLGSYITEQS 

       370        380        390        400        410        420 
LVFCQTVMST ELIDSVKSDM TIRGTPGELT YSVTYTPGAS TNKHPDWWNE KVKNHMMQHQ 

       430        440        450        460        470        480 
EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK 

       490        500        510        520        530        540 
EENKLWFSDK ITDAYNMPQP TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF 

       550        560        570        580        590        600 
MEPGLVLHLG GTHRMGFDEK EDNCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS 

       610        620 
LAIKSCEYIK QNFTPSPFTS EAQ

Q8J136 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools