Reviewed, UniProtKB/Swiss-Prot Q5B2E9 (P2OX_EMENI)

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
ORF Names:	AN5281

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Catalytic activity	D-glucose + O2 = 2-dehydro-D-glucose + H2O2.
Cofactor	Binds 1 FAD covalently per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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
	Chain	1 – 591	591	Pyranose 2-oxidase		PRO_0000205612
Sites
	Active site	495	1	By similarity
	Active site	548	1	By similarity
	Binding site	396	1	Substrate By similarity
	Binding site	398	1	Substrate By similarity
Amino acid modifications
	Modified residue	141	1	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5B2E9-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: D4A8B365C80B2542	FASTA	591	66,667
	10 20 30 40 50 60 MQYSRMTATR ENPKYKNLRV EECDVLSKGS TTNPRICGIK LNNSTVIGSG PVGATYAREI 70 80 90 100 110 120 LDPGSGASPG RKAPKVIMVE TGAQESKVPG EHKKNAVVYQ KHIDSFVNEK QNFNGQNKEQ 130 140 150 160 170 180 NIYHNLDANG VSRNVGGMST HWTCATPRQH ELERSKIFDD ATWDRLYKRA EELIGTRTDV 190 200 210 220 230 240 LDQSIRQRLV LDILRKKFKN RDAKALPLAA EKVEGKNLIK WSSSSTVLGN LLEDEKFTLL 250 260 270 280 290 300 DQHHCEKLEF NDETNKVSFA IIKNLAKPQT SKEDEDRLRI KAKYVIVCGG PILTPQLLFK 310 320 330 340 350 360 SGFRYDEEDA EDSEGNKSSL YIPALGRNLT EQTMCFCQIV LKDKWVEELQ KNNWGPECEE 370 380 390 400 410 420 HRRKYDEEDD PLRIPFDDLD PQVTLPFTEN TPWHTQIHRD AFSYGAVPPA IDKRTIVDLR 430 440 450 460 470 480 YFGRAETQWR NRVTFSKKLT DAYGMPQPTF DFKLSTKDRL ESHRMMQDME KVAGELGGYL 490 500 510 520 530 540 PGSEPQFLAP GLALHVCGTT AALRKGCRSE DEMKRISVCD ENSKVWGVEN LHLGGLNVIP 550 560 570 580 590 GPRSNASNPT LTAMCFAIKG AEEIRRKLGK KGSHSGNRDD GDVDTDTDDD A

References

[1]

"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACD01000093 Genomic DNA. Translation: EAA62441.1.
RefSeq	XP_662885.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2871572.
KEGG	ani:AN5281.2.
Enzyme and pathway databases
BRENDA	1.1.3.10. 3859.
Family and domain databases
InterPro	IPR000172. GMC_OxRdtase_N. [Graphical view]
PROSITE	PS00623. GMC_OXRED_1. False negative. PS00624. GMC_OXRED_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P2OX_EMENI

Accession

Primary (citable) accession number: Q5B2E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	April 26, 2005
Last modified:	September 22, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)