[1]	PROTEIN SEQUENCE. PubMed=9523716 [NCBI, ExPASy, EBI, Israel, Japan] Kiess M., Hecht H.-J., Kalisz H.M.; "Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases."; Eur. J. Biochem. 252:90-99(1998).
[2]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). DOI=10.1107/S0907444999003431; PubMed=10216293 [NCBI, ExPASy, EBI, Israel, Japan] Wohlfahrt G., Witt S., Hendle J., Schomburg D., Kalisz H.M., Hecht H.-J.; "1.8 and 1.9-A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes."; Acta Crystallogr. D 55:969-977(1999).

Comments

CATALYTIC ACTIVITY: Beta-D-glucose + O₂ = D-glucono-1,5-lactone + H₂O₂.
COFACTOR: FAD.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
MISCELLANEOUS: This enzyme is widely applied for the determination of glucose in body fluids and in removing residual glucose or oxygen from foods and beverages. Furthermore, glucose oxidase-producing moulds such as aspergillus and penicillium species are used for the biological production of gluconic acid.
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

3D structure databases

PDB

1GPE; X-ray; 1.80 A; A/B=1-587.

[ExPASy / RCSB / EBI]

PDBsum

1GPE; -.

ModBase

P81156.

Family and domain databases

InterPro

IPR012132; GMC_OxRdtase.
IPR000172; GMC_OxRdtase_N.
IPR007867; GMC_OxRtase_C.
Graphical view of domain structure.

Pfam

PF05199; GMC_oxred_C; 1.
PF00732; GMC_oxred_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000137; Alcohol_oxidase; 1.

PROSITE

PS00623; GMC_OXRED_1; 1.
PS00624; GMC_OXRED_2; 1.

Other

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

Keywords

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 587`	`587`	`Glucose oxidase.`	`PRO_0000205611`
`NP_BIND`	`26 55`	`30`	`FAD (Probable).`
`ACT_SITE`	`520 520`
`CARBOHYD`	`93 93`		`N-linked (GlcNAc...) (By similarity).`
`DISULFID`	`168 210`
`HELIX`	`10 12`	`3`
`HELIX`	`17 19`	`3`
`TURN`	`20 22`	`3`
`STRAND`	`24 30`	`7`
`HELIX`	`34 44`	`11`
`STRAND`	`51 57`	`7`
`HELIX`	`65 68`	`4`
`HELIX`	`70 72`	`3`
`TURN`	`73 78`	`6`
`HELIX`	`106 109`	`4`
`HELIX`	`120 128`	`9`
`HELIX`	`137 146`	`10`
`STRAND`	`148 150`	`3`
`HELIX`	`155 160`	`6`
`HELIX`	`166 168`	`3`
`STRAND`	`171 178`	`8`
`HELIX`	`189 199`	`11`
`STRAND`	`215 217`	`3`
`STRAND`	`220 223`	`4`
`HELIX`	`232 236`	`5`
`TURN`	`237 242`	`6`
`STRAND`	`246 251`	`6`
`STRAND`	`253 262`	`10`
`STRAND`	`265 276`	`12`
`STRAND`	`279 291`	`13`
`TURN`	`295 297`	`3`
`HELIX`	`298 304`	`7`
`HELIX`	`310 315`	`6`
`STRAND`	`321 323`	`3`
`STRAND`	`329 331`	`3`
`STRAND`	`334 342`	`9`
`HELIX`	`344 346`	`3`
`STRAND`	`351 357`	`7`
`HELIX`	`358 362`	`5`
`HELIX`	`363 365`	`3`
`HELIX`	`366 375`	`10`
`HELIX`	`377 386`	`10`
`HELIX`	`393 409`	`17`
`STRAND`	`413 420`	`8`
`STRAND`	`424 433`	`10`
`STRAND`	`438 445`	`8`
`HELIX`	`447 449`	`3`
`STRAND`	`452 455`	`4`
`HELIX`	`462 479`	`18`
`HELIX`	`484 487`	`4`
`STRAND`	`488 494`	`7`
`HELIX`	`495 497`	`3`
`HELIX`	`504 513`	`10`
`HELIX`	`530 532`	`3`
`STRAND`	`546 550`	`5`
`HELIX`	`565 585`	`21`

Sequence information

Length: 587 AA [This is the length of the unprocessed precursor]

Molecular weight: 63965 Da [This is the MW of the unprocessed precursor]

CRC64: 2827477B3DF4508C [This is a checksum on the sequence]

        10         20         30         40         50         60 
YLPAQQIDVQ SSLLSDPSKV AGKTYDYIIA GGGLTGLTVA AKLTENPKIK VLVIEKGFYE 

        70         80         90        100        110        120 
SNDGAIIEDP NAYGQIFGTT VDQNYLTVPL INNRTNNIKA GKGLGGSTLI NGDSWTRPDK 

       130        140        150        160        170        180 
VQIDSWEKVF GMEGWNWDNM FEYMKKAEAA RTPTAAQLAA GHSFNATCHG TNGTVQSGAR 

       190        200        210        220        230        240 
DNGQPWSPIM KALMNTVSAL GVPVQQDFLC GHPRGVSMIM NNLDENQVRV DAARAWLLPN 

       250        260        270        280        290        300 
YQRSNLEILT GQMVGKVLFK QTASGPQAVG VNFGTNKAVN FDVFAKHEVL LAAGSAISPL 

       310        320        330        340        350        360 
ILEYSGIGLK SVLDQANVTQ LLDLPVGINM QDQTTTTVSS RASSAGAGQG QAVFFANFTE 

       370        380        390        400        410        420 
TFGDYAPQAR DLLNTKLDQW AEETVARGGF HNVTALKVQY ENYRNWLLDE DVAFAELFMD 

       430        440        450        460        470        480 
TEGKINFDLW DLIPFTRGSV HILSSDPYLW QFANDPKFFL NEFDLLGQAA ASKLARDLTS 

       490        500        510        520        530        540 
QGAMKEYFAG ETLPGYNLVQ NATLSQWSDY VLQNFRPNWH AVSSCSMMSR ELGGVVDATA 

       550        560        570        580 
KVYGTQGLRV IDGSIPPTQV SSHVMTIFYG MALKVADAIL DDYAKSA

P81156 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