ID   P2OX_EMENI              Reviewed;         601 AA.
AC   Q5B2E9; C8VH04;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Pyranose 2-oxidase;
DE            Short=P2Ox;
DE            Short=POD;
DE            Short=POx;
DE            Short=PROD;
DE            Short=Pyranose oxidase;
DE            EC=1.1.3.10;
DE   AltName: Full=FAD-oxidoreductase;
DE   AltName: Full=Glucose 2-oxidase;
DE   AltName: Full=Pyranose:oxygen 2-oxidoreductase;
GN   Name=p2ox; ORFNames=AN5281;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Catalyzes the oxidation of various aldopyranoses and
CC       disaccharides on carbon-2 to the corresponding 2-keto sugars
CC       concomitant with the reduction of O(2) to H(2)O(2). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + O2 = 2-dehydro-D-glucose + H2O2;
CC         Xref=Rhea:RHEA:10552, ChEBI:CHEBI:4167, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16609; EC=1.1.3.10;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD covalently per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA62441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000093; EAA62441.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001305; CBF82183.1; -; Genomic_DNA.
DR   RefSeq; XP_662885.1; XM_657793.1.
DR   AlphaFoldDB; Q5B2E9; -.
DR   SMR; Q5B2E9; -.
DR   CAZy; AA3; Auxiliary Activities 3.
DR   EnsemblFungi; CBF82183; CBF82183; ANIA_05281.
DR   EnsemblFungi; EAA62441; EAA62441; AN5281.2.
DR   GeneID; 2871572; -.
DR   KEGG; ani:AN5281.2; -.
DR   VEuPathDB; FungiDB:AN5281; -.
DR   eggNOG; ENOG502R261; Eukaryota.
DR   HOGENOM; CLU_023699_0_0_1; -.
DR   InParanoid; Q5B2E9; -.
DR   OMA; QFMAPGL; -.
DR   OrthoDB; 592026at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050233; F:pyranose oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR012814; P2OX.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02462; pyranose_ox; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..601
FT                   /note="Pyranose 2-oxidase"
FT                   /id="PRO_0000205612"
FT   REGION          577..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        505
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   ACT_SITE        558
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         151
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   601 AA;  67853 MW;  06684035296A92B9 CRC64;
     MQYSRMTATR ENPKYKNLRV EECDVLIIGS GPVGATYARE ILDPGSGASP GRKAPKVIMV
     ETGAQESKVP GEHKKNAVVY QKHIDSFVNV IQGSLFATSV PTRVDPNLKL PPVSWSPREK
     QNFNGQNKEQ NIYHNLDANG VSRNVGGMST HWTCATPRQH ELERSKIFDD ATWDRLYKRA
     EELIGTRTDV LDQSIRQRLV LDILRKKFKN RDAKALPLAA EKVEGKNLIK WSSSSTVLGN
     LLEDEKFTLL DQHHCEKLEF NDETNKVSFA IIKNLAKPQT SKEDEDRLRI KAKYVIVCGG
     PILTPQLLFK SGFRYDEEDA EDSEGNKSSL YIPALGRNLT EQTMCFCQIV LKDKWVEELQ
     KNNWGPECEE HRRKYDEEDD PLRIPFDDLD PQVTLPFTEN TPWHTQIHRD AFSYGAVPPA
     IDKRTIVDLR YFGRAETQWR NRVTFSKKLT DAYGMPQPTF DFKLSTKDRL ESHRMMQDME
     KVAGELGGYL PGSEPQFLAP GLALHVCGTT AALRKGCRSE DEMKRISVCD ENSKVWGVEN
     LHLGGLNVIP GPRSNASNPT LTAMCFAIKG AEEIRRKLGK KGSHSGNRDD GDVDTDTDDD
     A