ID GOX_ASPNG Reviewed; 605 AA. AC P13006; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 04-NOV-2026, entry version 149. DE RecName: Full=Glucose oxidase {ECO:0000303|Ref.4}; DE Short=GOD {ECO:0000303|PubMed:2076553}; DE Short=GOx {ECO:0000303|PubMed:2792372}; DE EC=1.1.3.4 {ECO:0000269|PubMed:14188176, ECO:0000269|PubMed:14257628, ECO:0000269|PubMed:14299649, ECO:0000269|PubMed:2406261, ECO:0000269|PubMed:24283586, ECO:0000269|PubMed:28631058}; DE AltName: Full=Beta-D-glucose:oxygen 1-oxido-reductase {ECO:0000303|PubMed:2076553}; DE Flags: Precursor; GN Name=gox {ECO:0000303|PubMed:2792372}; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732; RX PubMed=2792372; DOI=10.1016/0014-5793(89)81061-0; RA Kriechbaum M., Heilmann H.J., Wientjes F.J., Hahn M., Jany K.-D., RA Gassen H.G., Sharif F., Alaeddinoglu G.; RT "Cloning and DNA sequence analysis of the glucose oxidase gene from RT Aspergillus niger NRRL-3."; RL FEBS Lett. 255:63-66(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, COFACTOR, CATALYTIC RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2406261; DOI=10.1016/s0021-9258(19)39664-4; RA Frederick K.R., Tung J., Emerick R.S., Masiarz F.R., Chamberlain S.H., RA Vasavada A., Rosenberg S., Chakraborty S., Schopter L.M., Massey V.; RT "Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion RT from Saccharomyces cerevisiae and kinetic analysis of a yeast-derived RT enzyme."; RL J. Biol. Chem. 265:3793-3802(1990). RN [3] RP NUCLEOTIDE SEQUENCE OF 1-32, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=2076553; DOI=10.1007/bf00327024; RA Whittington H., Kerry-Williams S., Bidgood K., Dodsworth N., Peberdy J., RA Dobson M., Hinchliffe E., Ballance D.J.; RT "Expression of the Aspergillus niger glucose oxidase gene in A. niger, A. RT nidulans and Saccharomyces cerevisiae."; RL Curr. Genet. 18:531-536(1990). RN [4] RP IDENTIFICATION, FUNCTION, AND CATALYTIC ACTIVITY. RA Muller D.; RT "Studies on the new enzyme glucoseoxidase. I."; RL Biochem. Z. 199:136-170(1928). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RA Muller D.; RT "Studies on the new enzyme glucoseoxidase. II."; RL Biochem. Z. 205:111-143(1929). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. RX PubMed=14188176; DOI=10.1021/bi00892a018; RA Pazur J.H., Kleppe K.; RT "The oxidation of glucose and related compounds by glucose oxidase from RT Aspergillus niger."; RL Biochemistry 3:578-583(1964). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. RX PubMed=14257628; DOI=10.1016/s0021-9258(18)91224-x; RA Gibson Q.H., Swoboda B.E.P., Massey V.; RT "Kinetics and mechanism of action of glucose oxidase."; RL J. Biol. Chem. 239:3927-3934(1964). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=14299649; DOI=10.1016/s0021-9258(18)97448-x; RA Swoboda B.E.P., Massey V.; RT "Purification and properties of the glucose oxidase from Aspergillus RT niger."; RL J. Biol. Chem. 240:2209-2215(1965). RN [9] RP CATALYTIC ACTIVITY. RX PubMed=4299571; DOI=10.1093/oxfordjournals.jbchem.a128776; RA Nakamura S., Ogura Y.; RT "Action mechanism of glucose oxidase of Aspergillus niger."; RL J. Biochem. 63:308-316(1968). RN [10] RP SUBUNIT, AND COFACTOR. RX PubMed=1213991; DOI=10.1093/oxfordjournals.jbchem.a130974; RA Tsuge H., Natsuaki O., Ohashi K.; RT "Purification, properties, and molecular features of glucose oxidase from RT Aspergillus niger."; RL J. Biochem. 78:835-843(1975). RN [11] RP GLYCOSYLATION. RX PubMed=2511903; DOI=10.1139/o89-072; RA Takegawa K., Fujiwara K., Iwahara S., Yamamoto K., Tochikura T.; RT "Effect of deglycosylation of N-linked sugar chains on glucose oxidase from RT Aspergillus niger."; RL Biochem. Cell Biol. 67:460-464(1989). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7826581; DOI=10.1016/0956-5663(94)80050-2; RA Luong J.H., Masson C., Brown R.S., Male K.B., Nguyen A.L.; RT "Monitoring the activity of glucose oxidase during the cultivation of RT Aspergillus niger using novel amperometric sensor with 1, 1'- RT dimethylferricinium as a mediator."; RL Biosens. Bioelectron. 9:577-584(1994). RN [13] RP BIOTECHNOLOGY. RX PubMed=31137288; DOI=10.4315/0362-028x-58.3.273; RA Dobbenie D., Uyttendaele M., Debevere J.; RT "Antibacterial Activity of the Glucose Oxidase/Glucose System in Liquid RT Whole Egg."; RL J. Food Prot. 58:273-279(1995). RN [14] RP BIOTECHNOLOGY. RX PubMed=10491329; DOI=10.1006/bbrc.1999.1330; RA D'Auria S., Herman P., Rossi M., Lakowicz J.R.; RT "The fluorescence emission of the apo-glucose oxidase from Aspergillus RT niger as probe to estimate glucose concentrations."; RL Biochem. Biophys. Res. Commun. 263:550-553(1999). RN [15] RP BIOTECHNOLOGY. RX PubMed=9469255; DOI=10.1016/s0009-8981(97)00151-4; RA Harborn U., Xie B., Venkatesh R., Danielsson B.; RT "Evaluation of a miniaturized thermal biosensor for the determination of RT glucose in whole blood."; RL Clin. Chim. Acta 267:225-237(1997). RN [16] RP BIOTECHNOLOGY. RX PubMed=11333029; DOI=10.1016/s0960-8524(01)00014-1; RA Kona R.P., Qureshi N., Pai J.S.; RT "Production of glucose oxidase using Aspergillus niger and corn steep RT liquor."; RL Bioresour. Technol. 78:123-126(2001). RN [17] RP BIOTECHNOLOGY. RX PubMed=11690697; DOI=10.1016/s0168-1656(01)00386-8; RA Tzanov T., Costa S.A., Guebitz G.M., Cavaco-Paulo A.; RT "Hydrogen peroxide generation with immobilized glucose oxidase for textile RT bleaching."; RL J. Biotechnol. 93:87-94(2002). RN [18] RP BIOTECHNOLOGY. RX PubMed=12764565; DOI=10.1007/s00253-002-1208-0; RA Malherbe D.F., du Toit M., Cordero Otero R.R., van Rensburg P., RA Pretorius I.S.; RT "Expression of the Aspergillus niger glucose oxidase gene in Saccharomyces RT cerevisiae and its potential applications in wine production."; RL Appl. Microbiol. Biotechnol. 61:502-511(2003). RN [19] RP BIOTECHNOLOGY. RX PubMed=15448967; DOI=10.1007/s00216-004-2770-3; RA Rossi L.M., Quach A.D., Rosenzweig Z.; RT "Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing."; RL Anal. Bioanal. Chem. 380:606-613(2004). RN [20] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15450808; DOI=10.1016/j.ab.2004.06.025; RA Karmali K., Karmali A., Teixeira A., Curto M.J.; RT "Assay for glucose oxidase from Aspergillus niger and Penicillium RT amagasakiense by Fourier transform infrared spectroscopy."; RL Anal. Biochem. 333:320-327(2004). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=16133329; DOI=10.1007/s00253-005-0031-9; RA Clarke K.G., Johnstone-Robertson M., Price B., Harrison S.T.; RT "Location of glucose oxidase during production by Aspergillus niger."; RL Appl. Microbiol. Biotechnol. 70:72-77(2006). RN [22] RP BIOTECHNOLOGY. RX PubMed=16889385; DOI=10.1021/bp060076k; RA Valdivieso-Ugarte M., Ronchel C., Banuelos O., Velasco J., Adrio J.L.; RT "Expression of an Aspergillus niger glucose oxidase in saccharomyces RT cerevisiae and its use to optimize fructo-oligosaccharides synthesis."; RL Biotechnol. Prog. 22:1096-1101(2006). RN [23] RP SUBCELLULAR LOCATION. RX PubMed=17787009; DOI=10.1002/bit.21642; RA Johnstone-Robertson M., Clarke K.G., Harrison S.T.; RT "Characterization of the distribution of glucose oxidase in Penicillium sp. RT CBS 120262 and Aspergillus niger NRRL-3 cultures and its effect on RT integrated product recovery."; RL Biotechnol. Bioeng. 99:910-918(2008). RN [24] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=24283586; DOI=10.1111/lam.12202; RA Meng Y., Zhao M., Yang M., Zhang Q., Hao J., Meng Y.; RT "Production and characterization of recombinant glucose oxidase from RT Aspergillus niger expressed in Pichia pastoris."; RL Lett. Appl. Microbiol. 58:393-400(2014). RN [25] RP BIOTECHNOLOGY. RX PubMed=25463642; DOI=10.1016/j.bios.2014.11.037; RA Wu C., Sun H., Li Y., Liu X., Du X., Wang X., Xu P.; RT "Biosensor based on glucose oxidase-nanoporous gold co-catalysis for RT glucose detection."; RL Biosens. Bioelectron. 66:350-355(2015). RN [26] RP MUTAGENESIS OF GLN-112; GLN-164; TYR-531; THR-576 AND LEU-591. RX PubMed=26642312; DOI=10.1371/journal.pone.0144289; RA Marin-Navarro J., Roupain N., Talens-Perales D., Polaina J.; RT "Identification and structural analysis of amino acid substitutions that RT increase the stability and activity of Aspergillus niger glucose oxidase."; RL PLoS ONE 10:e0144289-e0144289(2015). RN [27] RP BIOTECHNOLOGY. RX PubMed=28660924; DOI=10.1039/c7fd00042a; RA Golikova E.P., Lakina N.V., Grebennikova O.V., Matveeva V.G., Sulman E.M.; RT "A study of biocatalysts based on glucose oxidase."; RL Faraday Discuss. 202:303-314(2017). RN [28] RP REVIEW ON BIOTECHNOLOGY. RX PubMed=28659876; DOI=10.3389/fmicb.2017.01032; RA Dubey M.K., Zehra A., Aamir M., Meena M., Ahirwal L., Singh S., Shukla S., RA Upadhyay R.S., Bueno-Mari R., Bajpai V.K.; RT "Improvement Strategies, Cost Effective Production, and Potential RT Applications of Fungal Glucose Oxidase (GOD): Current Updates."; RL Front. Microbiol. 8:1032-1032(2017). RN [29] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=28631058; DOI=10.1007/s12033-017-0017-8; RA Khadivi Derakshan F., Darvishi F., Dezfulian M., Madzak C.; RT "Expression and characterization of glucose oxidase from Aspergillus niger RT in Yarrowia lipolytica."; RL Mol. Biotechnol. 59:307-314(2017). RN [30] RP BIOTECHNOLOGY. RX PubMed=29438880; DOI=10.1016/j.biomaterials.2018.02.004; RA Zhang R., Feng L., Dong Z., Wang L., Liang C., Chen J., Ma Q., Zhang R., RA Chen Q., Wang Y., Liu Z.; RT "Glucose & oxygen exhausting liposomes for combined cancer starvation and RT hypoxia-activated therapy."; RL Biomaterials 162:123-131(2018). RN [31] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=28939970; DOI=10.1007/s10529-017-2442-y; RA Zhu X., Sun J., Chu J.; RT "High-content screening of Aspergillus niger with both increased production RT and high secretion rate of glucose oxidase."; RL Biotechnol. Lett. 40:103-110(2018). RN [32] RP BIOTECHNOLOGY. RX PubMed=29051100; DOI=10.1016/j.ijbiomac.2017.10.074; RA Zhao B., Zhou L., Ma L., He Y., Gao J., Li D., Jiang Y.; RT "Co-immobilization of glucose oxidase and catalase in silica inverse opals RT for glucose removal from commercial isomaltooligosaccharide."; RL Int. J. Biol. Macromol. 107:2034-2043(2018). RN [33] RP BIOTECHNOLOGY, FUNCTION, ACTIVITY, AND MUTAGENESIS OF THR-32; ALA-58; RP ASN-157; ARG-167; GLY-296; THR-298; ALA-314; LEU-334; ARG-357; SER-362; RP HIS-388; GLU-389; GLU-396; VAL-442; SER-444 AND ASP-473. RX PubMed=31202848; DOI=10.1016/j.ijbiomac.2019.06.094; RA Mu Q., Cui Y., Tian Y., Hu M., Tao Y., Wu B.; RT "Thermostability improvement of the glucose oxidase from Aspergillus niger RT for efficient gluconic acid production via computational design."; RL Int. J. Biol. Macromol. 136:1060-1068(2019). RN [34] RP DISCOVERY. RX PubMed=33904729; DOI=10.1021/acs.analchem.1c01191; RA Heller A., Ulstrup J.; RT "Detlev Mueller's Discovery of Glucose Oxidase in 1925."; RL Anal. Chem. 93:7148-7149(2021). RN [35] RP BIOTECHNOLOGY. RX PubMed=33229152; DOI=10.1016/j.foodchem.2020.128639; RA Choi I., Zhong Q.; RT "Gluconic acid as a chelator to improve clarity of skim milk powder RT dispersions at pH 3.0."; RL Food Chem. 344:128639-128639(2021). RN [36] RP REVIEW ON BIOTECHNOLOGY. RX PubMed=35327664; DOI=10.3390/biom12030472; RA Bauer J.A., Zamocka M., Majtan J., Bauerova-Hlinkova V.; RT "Glucose oxidase, an enzyme 'Ferrari': its structure, function, production RT and properties in the light of various industrial and biotechnological RT applications."; RL Biomolecules 12:0-0(2022). RN [37] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=34500289; DOI=10.1016/j.foodchem.2021.130901; RA Zhong P., Zheng L., Yang Y., Zhou Y., Liu X., Yang Q., Ren J.; RT "Piezoelectric sensing of glucose oxidase activity of Aspergillus niger RT spores pretreated by different methods."; RL Food Chem. 370:130901-130901(2022). RN [38] RP CATALYTIC ACTIVITY. RX PubMed=36892276; DOI=10.1002/elps.202300010; RA Pruefer M., Stanke S., Bier F.F., Hoelzel R.; RT "Catalytic activity of glucose oxidase after dielectrophoretic RT immobilization on nanoelectrodes."; RL Electrophoresis 44:956-967(2023). RN [39] RP BIOTECHNOLOGY. RX PubMed=37326347; DOI=10.1111/1750-3841.16669; RA Shen D., Song G., Sun X., Fan F., Ding J., Fang Y., Li P.; RT "Effect of gluconic acid rinsing on cadmium decontamination from rice RT protein."; RL J. Food Sci. 88:3398-3409(2023). RN [40] {ECO:0007744|PDB:1GAL} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FAD, GLYCOSYLATION AT ASN-183; RP ASN-190; ASN-377 AND ASN-410, DISULFIDE BONDS, ACTIVE SITE, SUBUNIT, AND RP COFACTOR. RX PubMed=8421298; DOI=10.1006/jmbi.1993.1015; RA Hecht H.J., Kalisz H.M., Hendle J., Schmid R.D., Schomburg D.; RT "Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 RT A resolution."; RL J. Mol. Biol. 229:153-172(1993). RN [41] {ECO:0007744|PDB:1CF3} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FAD, COFACTOR, GLYCOSYLATION AT RP ASN-183; ASN-377 AND ASN-410, AND DISULFIDE BONDS. RX PubMed=10216293; DOI=10.1107/s0907444999003431; RA Wohlfahrt G., Witt S., Hendle J., Schomburg D., Kalisz H.M., Hecht H.J.; RT "1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and RT Aspergillus niger glucose oxidases as a basis for modelling substrate RT complexes."; RL Acta Crystallogr. D 55:969-977(1999). RN [42] {ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FAD, COFACTOR, GLYCOSYLATION AT RP ASN-183; ASN-377 AND ASN-410, AND DISULFIDE BONDS. RX PubMed=21568312; DOI=10.1021/bi200388g; RA Kommoju P.R., Chen Z.W., Bruckner R.C., Mathews F.S., Jorns M.S.; RT "Probing oxygen activation sites in two flavoprotein oxidases using RT chloride as an oxygen surrogate."; RL Biochemistry 50:5521-5534(2011). RN [43] {ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FAD, COFACTOR, GLYCOSYLATION AT RP ASN-183; ASN-280; ASN-377; ASN-410 AND ASN-495, ACTIVE SITE, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BONDS. RX PubMed=29291138; DOI=10.1021/acscatal.7b01575; RA Petrovic D., Frank D., Kamerlin S.C.L., Hoffmann K., Strodel B.; RT "Shuffling Active Site Substate Populations Affects Catalytic Activity: The RT Case of Glucose Oxidase."; RL ACS Catal. 7:6188-6197(2017). CC -!- FUNCTION: Glucose oxidase catalyzes the oxidation of beta-D-glucose to CC D-glucono-delta-lactone and hydrogen peroxide in the presence of CC molecular oxygen. D-glucono-delta-lactone is sequentially hydrolyzed by CC lactonase to D-gluconic acid, and the resulting hydrogen peroxide is CC hydrolyzed by catalase to oxygen and water (PubMed:14188176, CC PubMed:14257628, PubMed:14299649, PubMed:15450808, PubMed:2076553, CC PubMed:2406261, PubMed:24283586, PubMed:28631058, PubMed:28939970, CC PubMed:34500289, PubMed:7826581, Ref.4, Ref.5). The activity shows high CC specificity to beta-D-glucose, with very low to no activity towards L- CC glucose, 2-deoxy-D-glucose, 3-deoxy-D-glucose, 4-deoxy-D-glucose, 5- CC deoxy-D-glucose, 6-deoxy-D-glucose, 3-O-methyl-D-glucose, 4-O-methyl-D- CC glucose, 6-O-methyl-D-glucose, 4,6-O-benzylidene-D-glucose, 5-thio-5- CC deoxy-D-glucose, D-mannose, D-allose, D-galactose, D-fructose, D- CC arabinose, D-xylose, trehalose, melibiose, L-mannomethylose, lactose, CC sucrose or 1,5-anhydro-D-glucitol (PubMed:14188176, PubMed:14257628, CC PubMed:24283586, Ref.5). {ECO:0000269|PubMed:14188176, CC ECO:0000269|PubMed:14257628, ECO:0000269|PubMed:14299649, CC ECO:0000269|PubMed:15450808, ECO:0000269|PubMed:2076553, CC ECO:0000269|PubMed:2406261, ECO:0000269|PubMed:24283586, CC ECO:0000269|PubMed:28631058, ECO:0000269|PubMed:28939970, CC ECO:0000269|PubMed:34500289, ECO:0000269|PubMed:7826581, CC ECO:0000269|Ref.4, ECO:0000269|Ref.5}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2; CC Xref=Rhea:RHEA:11428, ChEBI:CHEBI:15379, ChEBI:CHEBI:15903, CC ChEBI:CHEBI:16217, ChEBI:CHEBI:16240; EC=1.1.3.4; CC Evidence={ECO:0000269|PubMed:14188176, ECO:0000269|PubMed:14257628, CC ECO:0000269|PubMed:14299649, ECO:0000269|PubMed:15450808, CC ECO:0000269|PubMed:2406261, ECO:0000269|PubMed:24283586, CC ECO:0000269|PubMed:28631058, ECO:0000269|PubMed:28939970, CC ECO:0000269|PubMed:34500289, ECO:0000269|PubMed:36892276, CC ECO:0000269|PubMed:4299571, ECO:0000269|PubMed:7826581}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11429; CC Evidence={ECO:0000269|PubMed:14188176, ECO:0000269|PubMed:14257628, CC ECO:0000269|PubMed:14299649, ECO:0000269|PubMed:2406261, CC ECO:0000269|PubMed:24283586, ECO:0000269|PubMed:28631058, CC ECO:0000269|PubMed:28939970, ECO:0000269|PubMed:34500289, CC ECO:0000269|PubMed:36892276, ECO:0000269|PubMed:4299571, CC ECO:0000269|PubMed:7826581}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:1213991, CC ECO:0000269|PubMed:14188176, ECO:0000269|PubMed:21568312, CC ECO:0000269|PubMed:2406261, ECO:0000269|PubMed:29291138, CC ECO:0000269|PubMed:8421298}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.12 M for beta-D-glucose {ECO:0000269|PubMed:14257628, CC ECO:0000269|PubMed:2406261, ECO:0000269|PubMed:24283586}; CC KM=0.025 M for 2-deoxy-D-glucose at 0 degrees Celsius CC {ECO:0000269|PubMed:14257628}; CC KM=0.04 M for 2-deoxy-D-glucose at 25 degrees Celsius CC {ECO:0000269|PubMed:14257628}; CC KM=0.26 mM for O(2) {ECO:0000269|PubMed:2406261}; CC Vmax=359 umol/min/mg enzyme towards D-glucose CC {ECO:0000269|PubMed:24283586}; CC pH dependence: CC Optimum pH is 5.5 to 6.0. {ECO:0000269|PubMed:14188176, CC ECO:0000269|PubMed:24283586, ECO:0000269|PubMed:28631058, CC ECO:0000269|Ref.5}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. CC {ECO:0000269|PubMed:28631058}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1213991, CC ECO:0000269|PubMed:8421298}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16133329, CC ECO:0000269|PubMed:17787009, ECO:0000269|PubMed:28939970}. Secreted, CC cell wall {ECO:0000269|PubMed:16133329, ECO:0000269|PubMed:17787009}. CC Cytoplasm {ECO:0000269|PubMed:16133329}. Secreted, extracellular space, CC extracellular matrix {ECO:0000269|PubMed:16133329, CC ECO:0000269|PubMed:17787009}. Note=The extracellular fluid contains 38% CC of the total activity with the remaining 62% being associated with the CC mycelia and distributed between the cell wall, cytoplasm and slime CC mucilage in the proportions of 34, 12 and 16%, respectively CC (PubMed:16133329). On progression from mid-exponential to stationary CC phase, the percentage of activity in the cytoplasm decreased 1.3-fold. CC Decreasing cytoplasmic activity is accompanied by 1.3-fold increases in CC the cell envelope and slime mucilage, with a 1.3-fold decrease in the CC extracellular fluid (PubMed:17787009). {ECO:0000269|PubMed:16133329, CC ECO:0000269|PubMed:17787009}. CC -!- PTM: The N-linked sugar chains of the glucose oxidase contributed to CC the high solubility of the enzyme in water. CC {ECO:0000269|PubMed:2511903}. CC -!- BIOTECHNOLOGY: The high specificity, high turnover and high stability CC of glucose oxidase make it an ideal enzyme for biosensor applications CC and such as the detection and quantitation of glucose in industrial CC solutions and body fluids (PubMed:10491329, PubMed:15448967, CC PubMed:25463642, PubMed:9469255). Glucose oxidase is used in the food CC industry for removal of residual glucose, e.g., desugaring of dried egg CC products, and as an antioxidant in the production of beer and soft CC drinks (PubMed:11333029, PubMed:12764565, PubMed:16889385, CC PubMed:29051100, PubMed:31137288, PubMed:31202848). In medicine, by CC consuming glucose, glucose oxidase could reduce the available metabolic CC energy sources of cancer cells, thereby, inhibiting their CC proliferation, and by consuming oxygen and producing gluconic acid, it CC could increase the hypoxia and acidity of the tumor microenvironment CC (PubMed:29438880, PubMed:35327664). Moreover, gluconic acid and its CC derivative salts can be used in a wide range of industries including CC textile dying, metal surface cleaning, food additives, detergents, CC concrete, cosmetics and pharmaceutical (PubMed:11690697, CC PubMed:28659876, PubMed:28660924, PubMed:33229152, PubMed:37326347). CC {ECO:0000269|PubMed:10491329, ECO:0000269|PubMed:11333029, CC ECO:0000269|PubMed:11690697, ECO:0000269|PubMed:12764565, CC ECO:0000269|PubMed:15448967, ECO:0000269|PubMed:16889385, CC ECO:0000269|PubMed:25463642, ECO:0000269|PubMed:28660924, CC ECO:0000269|PubMed:29051100, ECO:0000269|PubMed:29438880, CC ECO:0000269|PubMed:31137288, ECO:0000269|PubMed:31202848, CC ECO:0000269|PubMed:33229152, ECO:0000269|PubMed:37326347, CC ECO:0000269|PubMed:9469255, ECO:0000303|PubMed:28659876, CC ECO:0000303|PubMed:35327664}. CC -!- MISCELLANEOUS: Glucose oxidase was discovered by 26 years old Danish CC botanist Detlev Mueller in 1925. Detlev Mueller, at the then Royal CC Danish Veterinary and Agricultural University (KVL), published a brief CC note in a somewhat inaccessible journal reporting his discovery of a CC new enzyme, glucose oxidase (A new enzyme, glucose oxidase, from CC Aspergillus niger. Kgl. Veterinaer. og Landbohojskole Aarsskrift CC (Copenhagen) 1925, 329-331) (PubMed:33904729). Aspergillus niger CC glucose oxidase was the first flavoenzyme to be discovered, however, it CC was Nobel Prize winner Otto Warburg and Walter Christian, who in 1932- CC 1933 discovered a different enzyme, glucose 6-phosphate dehydrogenase, CC in baker's yeast Saccharomyces cerevisiae, that did recognize the CC significance of their enzyme's yellow cofactor (PubMed:33904729). CC {ECO:0000303|PubMed:33904729}. CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/GOP/"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Yellow - Issue 276 of CC January 2025; CC URL="https://www.proteinspotlight.org/back_issues/276/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X16061; CAA34197.1; -; Genomic_DNA. DR EMBL; J05242; AAA32695.1; -; mRNA. DR EMBL; X56443; CAA39826.1; -; Genomic_DNA. DR PIR; A35459; A35459. DR PDB; 1CF3; X-ray; 1.90 A; A=23-605. DR PDB; 1GAL; X-ray; 2.30 A; A=23-605. DR PDB; 3QVP; X-ray; 1.20 A; A=23-605. DR PDB; 3QVR; X-ray; 1.30 A; A=23-605. DR PDB; 5NIT; X-ray; 1.87 A; A=25-605. DR PDB; 5NIW; X-ray; 1.80 A; A=25-605. DR PDB; 9H7Z; X-ray; 1.71 A; A/M=1-605. DR AlphaFoldDB; P13006; -. DR SMR; P13006; -. DR CAZy; AA3; Auxiliary Activities 3. DR GlyCosmos; P13006; 8 sites, No reported glycans. DR ABCD; P13006; 1 sequenced antibody. DR VEuPathDB; FungiDB:An01g14740; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1132679; -. DR VEuPathDB; FungiDB:ATCC64974_11640; -. DR VEuPathDB; FungiDB:M747DRAFT_316207; -. DR eggNOG; KOG1238; Eukaryota. DR OMA; AKVNFDV; -. DR OrthoDB; 269227at2759; -. DR BioCyc; MetaCyc:MONOMER-17584; -. DR BRENDA; 1.1.3.4; 518. DR SABIO-RK; P13006; -. DR EvolutionaryTrace; P13006; -. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0046562; F:beta-D-glucose oxidase activity; EXP:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1. DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR027424; Glucose_Oxidase_domain_2. DR InterPro; IPR012132; GMC_OxRdtase. DR InterPro; IPR000172; GMC_OxRdtase_N. DR InterPro; IPR007867; GMC_OxRtase_C. DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1. DR PANTHER; PTHR11552:SF201; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR PIRSF; PIRSF000137; Alcohol_oxidase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. DR PCDDB; P13006; -. PE 1: Evidence at protein level; KW 3D-structure; Cell wall; Cytoplasm; Direct protein sequencing; KW Disulfide bond; Extracellular matrix; FAD; Flavoprotein; Glycoprotein; KW Oxidoreductase; Secreted; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..605 FT /note="Glucose oxidase" FT /id="PRO_0000012338" FT ACT_SITE 538 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:8421298, FT ECO:0007744|PDB:1GAL" FT BINDING 51 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR" FT BINDING 72 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 125 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 129 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 130 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0007744|PDB:1CF3, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 132 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 272 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 559 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000269|PubMed:29291138, FT ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW" FT BINDING 560 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000269|PubMed:29291138, FT ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW" FT BINDING 571 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT BINDING 583 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 183 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, FT ECO:0000269|PubMed:29291138, ECO:0000269|PubMed:8421298, FT ECO:0007744|PDB:1CF3, ECO:0007744|PDB:1GAL, FT ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR, FT ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000269|PubMed:29291138, ECO:0007744|PDB:1GAL" FT CARBOHYD 280 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000269|PubMed:29291138, ECO:0007744|PDB:5NIW" FT CARBOHYD 377 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, FT ECO:0000269|PubMed:29291138, ECO:0000269|PubMed:8421298, FT ECO:0007744|PDB:1CF3, ECO:0007744|PDB:1GAL, FT ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR, FT ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW" FT CARBOHYD 410 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, FT ECO:0000269|PubMed:29291138, ECO:0000269|PubMed:8421298, FT ECO:0007744|PDB:1CF3, ECO:0007744|PDB:1GAL, FT ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR, FT ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW" FT CARBOHYD 495 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498, FT ECO:0007744|PDB:5NIW" FT DISULFID 186..228 FT /evidence="ECO:0000269|PubMed:10216293, FT ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, FT ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, FT ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, FT ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, FT ECO:0007744|PDB:5NIW" FT MUTAGEN 32 FT /note="T->K: Stabilizes the enzyme structure by the FT introduction of new hydrogen salt bridge interaction." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 58 FT /note="A->M: Fills the deeply buried cavity in the vicinity FT of the FAD binding site, making the binding state more FT stable and thus contributing to stability." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 112 FT /note="Q->R: Increases significantly the enzyme's thermal FT stability by introducing a new salt bridge near the FT interphase of the dimeric protein structure; when FT associated with E-531." FT /evidence="ECO:0000269|PubMed:26642312" FT MUTAGEN 157 FT /note="N->K: Stabilizes the enzyme structure by the FT introduction of new hydrogen salt bridge interaction." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 164 FT /note="Q->R: Does not affect stability but causes a twofold FT increase of the enzyme's specific activity; when associated FT with E-591." FT /evidence="ECO:0000269|PubMed:26642312" FT MUTAGEN 167 FT /note="R->N: Stabilizes the enzyme structure by the FT introduction of new hydrogen bonding." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 296 FT /note="G->S: Optimizes the charge-charge interactions at FT the surface of the protein 3D-structure." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 298 FT /note="T->R: Stabilizes the enzyme structure by the FT introduction of new hydrogen bonding." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 314 FT /note="A->M: Fills the deeply buried cavity in the vicinity FT of the FAD binding site, making the binding state more FT stable and thus contributing to stability." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 334 FT /note="L->Y: Contributes to facilitate the inter-helix FT hydrophobic interaction." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 357 FT /note="R->T: Stabilizes the enzyme structure by the FT introduction of new hydrogen bonding." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 362 FT /note="S->P: Causes entropic stabilization, in which a FT proline contributes to enzyme rigidity due to the lower FT degree of freedom of proline in the unfolded state." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 388 FT /note="H->Q: Stabilizes the enzyme structure by the FT introduction of new hydrogen bonding." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 389 FT /note="E->Y: Stabilizes the enzyme structure by the FT introduction of new hydrogen bonding." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 396 FT /note="E->Q: Optimizes the charge-charge interactions at FT the surface of the protein 3D-structure." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 442 FT /note="V->G: Optimizes the charge-charge interactions at FT the surface of the protein 3D-structure." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 444 FT /note="S->N: Stabilizes the enzyme structure by the FT introduction of new hydrogen bonding." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 473 FT /note="D->N: Optimizes the charge-charge interactions at FT the surface of the protein 3D-structure." FT /evidence="ECO:0000269|PubMed:31202848" FT MUTAGEN 531 FT /note="Y->E: Increases significantly the enzyme's thermal FT stability by introducing a new salt bridge near the FT interphase of the dimeric protein structure; when FT associated with R-112." FT /evidence="ECO:0000269|PubMed:26642312" FT MUTAGEN 576 FT /note="T->M: Increases significantly the enzyme's thermal FT stability by generating a sulfur-pi interaction." FT /evidence="ECO:0000269|PubMed:26642312" FT MUTAGEN 591 FT /note="L->E: Does not affect stability but causes a twofold FT increase of the enzyme's specific activity; when associated FT with R-164." FT /evidence="ECO:0000269|PubMed:26642312" FT HELIX 26..29 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:3QVP" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 51..60 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:3QVP" FT TURN 90..95 FT /evidence="ECO:0007829|PDB:3QVP" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 124..127 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 138..146 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 155..165 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 173..178 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 189..196 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 207..216 FT /evidence="ECO:0007829|PDB:3QVP" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 251..255 FT /evidence="ECO:0007829|PDB:3QVP" FT TURN 256..260 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 271..278 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 285..294 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 298..309 FT /evidence="ECO:0007829|PDB:3QVP" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 316..322 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 328..331 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:3QVR" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:3QVR" FT STRAND 352..360 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 369..375 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 376..380 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 384..393 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 395..404 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 411..427 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 431..438 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 442..451 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 456..463 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 465..467 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 470..473 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 480..497 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 502..505 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 506..512 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 522..528 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 529..531 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 548..550 FT /evidence="ECO:0007829|PDB:3QVP" FT STRAND 558..560 FT /evidence="ECO:0007829|PDB:1CF3" FT STRAND 564..568 FT /evidence="ECO:0007829|PDB:3QVP" FT HELIX 583..603 FT /evidence="ECO:0007829|PDB:3QVP" SQ SEQUENCE 605 AA; 65638 MW; 25243E5ED1D2773B CRC64; MQTLLVSSLV VSLAAALPHY IRSNGIEASL LTDPKDVSGR TVDYIIAGGG LTGLTTAARL TENPNISVLV IESGSYESDR GPIIEDLNAY GDIFGSSVDH AYETVELATN NQTALIRSGN GLGGSTLVNG GTWTRPHKAQ VDSWETVFGN EGWNWDNVAA YSLQAERARA PNAKQIAAGH YFNASCHGVN GTVHAGPRDT GDDYSPIVKA LMSAVEDRGV PTKKDFGCGD PHGVSMFPNT LHEDQVRSDA AREWLLPNYQ RPNLQVLTGQ YVGKVLLSQN GTTPRAVGVE FGTHKGNTHN VYAKHEVLLA AGSAVSPTIL EYSGIGMKSI LEPLGIDTVV DLPVGLNLQD QTTATVRSRI TSAGAGQGQA AWFATFNETF GDYSEKAHEL LNTKLEQWAE EAVARGGFHN TTALLIQYEN YRDWIVNHNV AYSELFLDTA GVASFDVWDL LPFTRGYVHI LDKDPYLHHF AYDPQYFLNE LDLLGQAAAT QLARNISNSG AMQTYFAGET IPGDNLAYDA DLSAWTEYIP YHFRPNYHGV GTCSMMPKEM GGVVDNAARV YGVQGLRVID GSIPPTQMSS HVMTVFYAMA LKISDAILED YASMQ //