[1]	NUCLEOTIDE SEQUENCE [MRNA]. Takakura Y., Tsutsumi F., Inoue Y., Kuwata S.; "Identification and cloning of a novel pyranose oxidase with high catalytic activity from Lyophyllum shimeji and its expression in Escherichia coli."; Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.

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) (By similarity).
CATALYTIC ACTIVITY: D-glucose + O₂ = 2-dehydro-D-glucose + H₂O₂.
COFACTOR: Binds 1 FAD covalently per subunit (By similarity).
SUBUNIT: Homotetramer (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

AB119106; BAD12079.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q75ZP8.

Family and domain databases

InterPro

IPR000172; GMC_OxRdtase_N.
IPR012814; Pyranose_ox.
Graphical view of domain structure.

Pfam

PF00732; GMC_oxred_N; 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

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

Keywords

FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 618`	`618`	`Pyranose 2-oxidase.`	`PRO_0000205613`
`ACT_SITE`	`540 540`		`By similarity.`
`ACT_SITE`	`583 583`		`By similarity.`
`BINDING`	`441 441`		`Substrate (By similarity).`
`BINDING`	`443 443`		`Substrate (By similarity).`
`MOD_RES`	`170 170`		`Tele-8alpha-FAD histidine (By similarity).`

Sequence information

Length: 618 AA [This is the length of the unprocessed precursor]

Molecular weight: 68488 Da [This is the MW of the unprocessed precursor]

CRC64: 255B99DF266BC541 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLSTEQMLR DYPRSMQING QIPKNAIHET YGNDGVDVFI AGSGPIGATY AKLCVEAGLR 

        70         80         90        100        110        120 
VVMVEIGAAD SFYAVNAEEG TAVPYVPGYH KKNEIEFQKD IDRFVNVIKG ALQQVSVPVR 

       130        140        150        160        170        180 
NQNVPTLDPG AWSAPPGSSA ISNGKNPHQR EFENLSAEAV TRGVGGMSTH WTCSTPRIHP 

       190        200        210        220        230        240 
PMESLPGIGR PKLSNDPAED DKEWNELYSE AERLIGTSTK EFDESIRHTL VLRSLQDAYK 

       250        260        270        280        290        300 
DRQRIFRPLP LACHRLKNAP EYVEWHSAEN LFHSIYNDDK QKKLFTLLTN HRCTRLALTG 

       310        320        330        340        350        360 
GYEKKIGAAE VRNLLATRNP SSQLDSYIMA KVYVLASGAI GNPQILYNSG FSGLQVTPRN 

       370        380        390        400        410        420 
DSLIPNLGRY ITEQPMAFCQ IVLRQEFVDS VRDDPYGLPW WKEAVAQHIA KNPTDALPIP 

       430        440        450        460        470        480 
FRDPEPQVTT PFTEEHPWHT QIHRDAFSYG AVGPEVDSRV IVDLRWFGAT DPEANNLLVF 

       490        500        510        520        530        540 
QNDVQDGYSM PQPTFRYRPS TASNVRARKM MADMCEVASN LGGYLPTSPP QFMDPGLALH 

       550        560        570        580        590        600 
LAGTTRIGFD KATTVADNNS LVWDFANLYV AGNGTIRTGF GENPTLTSMC HAIKSARSII 

       610 
NTLKGGTDGK NTGEHRNL

Q75ZP8 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