ID OXDA_RHOTO Reviewed; 368 AA. AC P80324; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 114. DE RecName: Full=D-amino-acid oxidase {ECO:0000303|PubMed:8100225}; DE Short=DAAO {ECO:0000303|PubMed:8100225}; DE Short=DAMOX; DE Short=DAO; DE EC=1.4.3.3 {ECO:0000269|PubMed:12208501, ECO:0000269|PubMed:15058991, ECO:0000269|PubMed:15310841, ECO:0000269|PubMed:17145127, ECO:0000269|PubMed:8100225, ECO:0000269|PubMed:9383984, ECO:0000269|Ref.14, ECO:0000305|PubMed:12021281}; DE Flags: Precursor; GN Name=DAO1; OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula. OX NCBI_TaxID=5286; RN [1] RP PROTEIN SEQUENCE. RA Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S.; RT "The primary structure of D-amino acid oxidase from Rhodotorula gracilis."; RL Biotechnol. Lett. 17:193-198(1995). RN [2] {ECO:0000312|EMBL:AAB51107.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY. RC STRAIN=ATCC 26217 / Pan {ECO:0000303|PubMed:9383984}; RX PubMed=9383984; DOI=10.1016/s0168-1656(97)00142-9; RA Pollegioni L., Molla G., Campaner S., Martegani E., Pilone M.S.; RT "Cloning, sequencing and expression in E. coli of a D-amino acid oxidase RT cDNA from Rhodotorula gracilis active on cephalosporin C."; RL J. Biotechnol. 58:115-123(1997). RN [3] {ECO:0000312|EMBL:CAA96323.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26217 / Pan; RX PubMed=9579082; DOI=10.1099/00221287-144-4-1095; RA Alonso J., Barredo J.L., Diez B., Salto F., Garcia J.L., Cortes E.; RT "D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium RT toruloides) ATCC 26217."; RL Microbiology 144:1095-1101(1998). RN [4] {ECO:0000312|EMBL:AAB93974.1, ECO:0000312|EMBL:AAB93975.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 10788 / CBS 14 / BCRC 20306 / IAM 13469 / JCM 10020 / NBRC RC 0559 / NRRL Y-1091; RA Liaw G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=1680680; RA Perotti M.E., Pollegioni L., Pilone M.S.; RT "Expression of D-amino acid oxidase in Rhodotorula gracilis under induction RT conditions: a biochemical and cytochemical study."; RL Eur. J. Cell Biol. 55:104-113(1991). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=8100225; DOI=10.1016/s0021-9258(19)85181-5; RA Pollegioni L., Langkau B., Tischer W., Ghisla S., Pilone M.S.; RT "Kinetic mechanism of D-amino acid oxidases from Rhodotorula gracilis and RT Trigonopsis variabilis."; RL J. Biol. Chem. 268:13850-13857(1993). RN [7] RP BIOTECHNOLOGY. RX PubMed=7654197; DOI=10.1042/bj3100577; RA Pollegioni L., Ceciliani F., Curti B., Ronchi S., Pilone M.S.; RT "Studies on the structural and functional aspects of Rhodotorula gracilis RT D-amino acid oxidase by limited trypsinolysis."; RL Biochem. J. 310:577-583(1995). RN [8] RP BIOTECHNOLOGY. RX PubMed=9472778; DOI=10.1089/hum.1998.9.2-185; RA Stegman L.D., Zheng H., Neal E.R., Ben-Yoseph O., Pollegioni L., RA Pilone M.S., Ross B.D.; RT "Induction of cytotoxic oxidative stress by D-alanine in brain tumor cells RT expressing Rhodotorula gracilis D-amino acid oxidase: a cancer gene therapy RT strategy."; RL Hum. Gene Ther. 9:185-193(1998). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF RP 308-SER--LYS-321. RX PubMed=12208501; DOI=10.1016/s0014-5793(02)03111-3; RA Piubelli L., Caldinelli L., Molla G., Pilone M.S., Pollegioni L.; RT "Conversion of the dimeric D-amino acid oxidase from Rhodotorula gracilis RT to a monomeric form. A rational mutagenesis approach."; RL FEBS Lett. 526:43-48(2002). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBUNIT, AND MUTAGENESIS OF MET-213. RX PubMed=12021281; DOI=10.1074/jbc.m203946200; RA Sacchi S., Lorenzi S., Molla G., Pilone M.S., Rossetti C., Pollegioni L.; RT "Engineering the substrate specificity of D-amino-acid oxidase."; RL J. Biol. Chem. 277:27510-27516(2002). RN [11] RP INDUCTION. RX PubMed=12961754; DOI=10.1002/yea.1023; RA Molla G., Motteran L., Piubelli L., Pilone M.S., Pollegioni L.; RT "Regulation of D-amino acid oxidase expression in the yeast Rhodotorula RT gracilis."; RL Yeast 20:1061-1069(2003). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=15058991; DOI=10.1021/bp034206q; RA Pollegioni L., Caldinelli L., Molla G., Sacchi S., Pilone M.S.; RT "Catalytic properties of D-amino acid oxidase in cephalosporin C RT bioconversion: a comparison between proteins from different sources."; RL Biotechnol. Prog. 20:467-473(2004). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RP MUTAGENESIS OF THR-60; LEU-118; GLN-144; LYS-152; GLY-199; MET-213; RP TYR-223; ASP-242; GLN-253; ASP-304 AND HIS-329. RX PubMed=15310841; DOI=10.1093/protein/gzh064; RA Sacchi S., Rosini E., Molla G., Pilone M.S., Pollegioni L.; RT "Modulating D-amino acid oxidase substrate specificity: production of an RT enzyme for analytical determination of all D-amino acids by directed RT evolution."; RL Protein Eng. Des. Sel. 17:517-525(2004). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, RP AND MUTAGENESIS OF MET-213. RX DOI=10.1002/adsc.200606188; RA Caligiuri A., D'Arrigo P., Rosini E., Tessaro D., Molla G., Servi S., RA Pollegioni L.; RT "Enzymatic Conversion of Unnatural Amino Acids by Yeast D-Amino Acid RT Oxidase."; RL Adv. Synth. Catal. 348:2183-2190(2006). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP BIOTECHNOLOGY, AND MUTAGENESIS OF MET-213; TYR-223; TYR-238; SER-335 AND RP GLN-339. RX PubMed=17145127; DOI=10.1016/j.biochi.2006.10.017; RA Boselli A., Piubelli L., Molla G., Pilone M.S., Pollegioni L., Sacchi S.; RT "Investigating the role of active site residues of Rhodotorula gracilis D- RT amino acid oxidase on its substrate specificity."; RL Biochimie 89:360-368(2007). RN [16] RP BIOTECHNOLOGY. RX PubMed=18229946; DOI=10.1021/ac702230w; RA Pernot P., Mothet J.P., Schuvailo O., Soldatkin A., Pollegioni L., RA Pilone M., Adeline M.T., Cespuglio R., Marinesco S.; RT "Characterization of a yeast D-amino acid oxidase microbiosensor for D- RT serine detection in the central nervous system."; RL Anal. Chem. 80:1589-1597(2008). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=18343336; DOI=10.1263/jbb.105.110; RA Kuan I., Liao R., Hsieh H., Chen K., Yu C.; RT "Properties of Rhodotorula gracilis D-amino acid oxidase immobilized on RT magnetic beads through his-tag."; RL J. Biosci. Bioeng. 105:110-115(2008). RN [18] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, RP AND MUTAGENESIS OF SER-19; SER-120; GLN-144; LYS-321 AND ALA-345. RX PubMed=19694805; DOI=10.1111/j.1742-4658.2009.07191.x; RA Rosini E., Pollegioni L., Ghisla S., Orru R., Molla G.; RT "Optimization of D-amino acid oxidase for low substrate RT concentrations--towards a cancer enzyme therapy."; RL FEBS J. 276:4921-4932(2009). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=21053050; DOI=10.1007/s10529-010-0456-9; RA Abad S., Nahalka J., Winkler M., Bergler G., Speight R., Glieder A., RA Nidetzky B.; RT "High-level expression of Rhodotorula gracilis D-amino acid oxidase in RT Pichia pastoris."; RL Biotechnol. Lett. 33:557-563(2011). RN [20] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=26132227; DOI=10.1371/journal.pone.0131865; RA Chang Y.C., Khanal Lamichhane A., Bradley J., Rodgers L., RA Ngamskulrungroj P., Kwon-Chung K.J.; RT "Differences between Cryptococcus neoformans and Cryptococcus gattii in the RT Molecular Mechanisms Governing Utilization of D-Amino Acids as the Sole RT Nitrogen Source."; RL PLoS ONE 10:e0131865-e0131865(2015). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, RP AND MUTAGENESIS OF GLN-144. RX PubMed=34174417; DOI=10.1016/j.nano.2021.102424; RA Rosini E., Volpi N.A., Ziffels B., Grimaldi A., Sacchi S., Neri D., RA Pollegioni L.; RT "An antibody-based enzymatic therapy for cancer treatment: The selective RT localization of D-amino acid oxidase to EDA fibronectin."; RL Nanomedicine 36:102424-102424(2021). RN [22] {ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, ECO:0007744|PDB:1C0P} RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-361 IN COMPLEXES WITH FAD; RP D-ALANINE; 2-AMINOBENZOIC ACID AND LACTATE, COFACTOR, AND ENZYME MECHANISM. RX PubMed=11070076; DOI=10.1073/pnas.97.23.12463; RA Umhau S., Pollegioni L., Molla G., Diederichs K., Welte W., Pilone M.S., RA Ghisla S.; RT "The X-ray structure of D-amino acid oxidase at very high resolution RT identifies the chemical mechanism of flavin-dependent substrate RT dehydrogenation."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12463-12468(2000). RN [23] {ECO:0007744|PDB:1C0I} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-361 IN COMPLEX WITH FAD AND RP ANTHRANILATE, COFACTOR, AND SUBUNIT. RX PubMed=12445787; DOI=10.1016/s0022-2836(02)01062-8; RA Pollegioni L., Diederichs K., Molla G., Umhau S., Welte W., Ghisla S., RA Pilone M.S.; RT "Yeast D-amino acid oxidase: structural basis of its catalytic RT properties."; RL J. Mol. Biol. 324:535-546(2002). CC -!- FUNCTION: Catalyzes the oxidative deamination of D-amino acids with CC broad substrate specificity (PubMed:12021281, PubMed:12208501, CC PubMed:15058991, PubMed:15310841, PubMed:17145127, PubMed:18343336, CC PubMed:19694805, PubMed:21053050, PubMed:26132227, PubMed:34174417, CC PubMed:8100225, PubMed:9383984, Ref.14). Enables the organism to CC utilize D-amino acids as a source of nutrients (By similarity). CC {ECO:0000250|UniProtKB:Q9HGY3, ECO:0000269|PubMed:12021281, CC ECO:0000269|PubMed:12208501, ECO:0000269|PubMed:15058991, CC ECO:0000269|PubMed:15310841, ECO:0000269|PubMed:17145127, CC ECO:0000269|PubMed:18343336, ECO:0000269|PubMed:19694805, CC ECO:0000269|PubMed:21053050, ECO:0000269|PubMed:26132227, CC ECO:0000269|PubMed:34174417, ECO:0000269|PubMed:8100225, CC ECO:0000269|PubMed:9383984, ECO:0000269|Ref.14}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a D-alpha-amino acid + O2 + H2O = a 2-oxocarboxylate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, CC ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:12208501, CC ECO:0000269|PubMed:15058991, ECO:0000269|PubMed:15310841, CC ECO:0000269|PubMed:17145127, ECO:0000269|PubMed:18343336, CC ECO:0000269|PubMed:19694805, ECO:0000269|PubMed:21053050, CC ECO:0000269|PubMed:26132227, ECO:0000269|PubMed:34174417, CC ECO:0000269|PubMed:8100225, ECO:0000269|PubMed:9383984, CC ECO:0000269|Ref.14, ECO:0000305|PubMed:12021281}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; CC Evidence={ECO:0000269|PubMed:12208501, ECO:0000269|PubMed:15058991, CC ECO:0000269|PubMed:15310841, ECO:0000269|PubMed:17145127, CC ECO:0000269|PubMed:18343336, ECO:0000269|PubMed:19694805, CC ECO:0000269|PubMed:21053050, ECO:0000269|PubMed:26132227, CC ECO:0000269|PubMed:34174417, ECO:0000269|PubMed:8100225, CC ECO:0000269|PubMed:9383984, ECO:0000269|Ref.14, CC ECO:0000305|PubMed:12021281}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-leucine + O2 + H2O = 4-methyl-2-oxopentanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:143079; Evidence={ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; CC Evidence={ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-alanine + O2 + H2O = pyruvate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:57416; Evidence={ECO:0000269|PubMed:12208501, CC ECO:0000269|PubMed:15058991, ECO:0000269|PubMed:15310841, CC ECO:0000269|PubMed:17145127, ECO:0000269|PubMed:18343336, CC ECO:0000269|PubMed:19694805, ECO:0000269|PubMed:21053050, CC ECO:0000269|PubMed:26132227, ECO:0000269|PubMed:34174417, CC ECO:0000269|PubMed:8100225, ECO:0000269|PubMed:9383984, CC ECO:0000269|Ref.14, ECO:0000305|PubMed:12021281}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; CC Evidence={ECO:0000269|PubMed:12208501, ECO:0000269|PubMed:15058991, CC ECO:0000269|PubMed:15310841, ECO:0000269|PubMed:17145127, CC ECO:0000269|PubMed:18343336, ECO:0000269|PubMed:19694805, CC ECO:0000269|PubMed:21053050, ECO:0000269|PubMed:26132227, CC ECO:0000269|PubMed:34174417, ECO:0000269|PubMed:8100225, CC ECO:0000269|PubMed:9383984, ECO:0000269|Ref.14, CC ECO:0000305|PubMed:12021281}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glutamate + O2 + H2O = 2-oxoglutarate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:10028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29986; Evidence={ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10029; CC Evidence={ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-histidine + O2 + H2O = 3-(imidazol-5-yl)pyruvate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:78227, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58133, CC ChEBI:CHEBI:142967; Evidence={ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78228; CC Evidence={ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-proline + O2 = 1-pyrroline-2-carboxylate + H2O2; CC Xref=Rhea:RHEA:78259, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:39785, ChEBI:CHEBI:57726; CC Evidence={ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78260; CC Evidence={ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-methionine + O2 + H2O = 4-methylsulfanyl-2-oxobutanoate + CC H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; CC Evidence={ECO:0000269|PubMed:12021281, ECO:0000269|PubMed:21053050, CC ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; CC Evidence={ECO:0000269|PubMed:12021281, ECO:0000269|PubMed:21053050, CC ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-arginine + O2 + H2O = 5-guanidino-2-oxopentanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:78219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32689, CC ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:15310841, CC ECO:0000269|PubMed:17145127}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78220; CC Evidence={ECO:0000269|PubMed:15310841, ECO:0000269|PubMed:17145127}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-valine + O2 + H2O = 3-methyl-2-oxobutanoate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:78203, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:74338; Evidence={ECO:0000269|PubMed:26132227, CC ECO:0000269|PubMed:8100225}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78204; CC Evidence={ECO:0000269|PubMed:26132227, ECO:0000269|PubMed:8100225}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-threonine + O2 + H2O = (S)-3-hydroxy-2-oxobutanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:78251, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57757, CC ChEBI:CHEBI:228256; Evidence={ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78252; CC Evidence={ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-serine + O2 + H2O = 3-hydroxypyruvate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:26132227}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; CC Evidence={ECO:0000269|PubMed:26132227}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-tryptophan + O2 + H2O = indole-3-pyruvate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:78247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:57719; Evidence={ECO:0000269|PubMed:12208501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78248; CC Evidence={ECO:0000269|PubMed:12208501}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:11070076, ECO:0000269|PubMed:12021281, CC ECO:0000269|PubMed:12208501, ECO:0000269|PubMed:12445787, CC ECO:0000269|PubMed:17145127}; CC -!- ACTIVITY REGULATION: Inhibited by high concentrations of hydrogen CC peroxide. {ECO:0000269|PubMed:15058991, ECO:0000269|PubMed:18343336}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.9 mM for D-alanine using free enzyme (at 25 degrees Celsius and CC at pH 8) {ECO:0000269|PubMed:18343336}; CC KM=1.6 mM for D-alanine using immobilized enzyme (at 25 degrees CC Celsius and at pH 8) {ECO:0000269|PubMed:18343336}; CC KM=0.8 mM for D-alanine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281, ECO:0000269|PubMed:17145127, CC ECO:0000269|PubMed:19694805, ECO:0000269|PubMed:34174417}; CC KM=0.9 mM for D-alanine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|Ref.14}; CC KM=2.6 mM for D-alanine (at 15 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:19694805}; CC KM=1 mM for D-alanine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:15058991, ECO:0000269|PubMed:9383984}; CC KM=21.5 mM for D-proline (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281}; CC KM=14.4 mM for D-asparagine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281}; CC KM=4.6 mM for D-glutamine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281}; CC KM=0.2 mM for D-methionine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281}; CC KM=18 mM for D-aspartate (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281, ECO:0000269|PubMed:17145127}; CC KM=33.1 mM for D-aspartate (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:15310841}; CC KM=77.3 mM for D-glutamate (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:12021281}; CC KM=2.8 mM for D-arginine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:15310841}; CC KM=18 mM for D-arginine (at 25 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:17145127}; CC KM=5 mM for cephalosporin C (CPC) (at 25 degrees Celsius and at pH CC 8.5) {ECO:0000269|PubMed:17145127, ECO:0000269|PubMed:9383984}; CC KM=4 mM for cephalosporin C (CPC) (at 25 degrees Celsius and at pH CC 8.5) {ECO:0000269|PubMed:15058991}; CC KM=0.04 mM for 3-(2-Naphthyl)-D-alanine (at 25 degrees Celsius and at CC pH 8.5) {ECO:0000269|Ref.14}; CC KM=0.04 mM for 3-(1-Naphthyl)-D-alanine (at 25 degrees Celsius and at CC pH 8.5) {ECO:0000269|Ref.14}; CC KM=0.01 mM for d-2-Naphthylglycine (at 25 degrees Celsius and at pH CC 8.5) {ECO:0000269|Ref.14}; CC KM=0.33 mM for d-1-Naphthylglycine (at 25 degrees Celsius and at pH CC 8.5) {ECO:0000269|Ref.14}; CC KM=1.9 mM for oxygen (at 15 degrees Celsius and at pH 8.5) CC {ECO:0000269|PubMed:19694805}; CC Note=kcat is 52.4 sec(-1) with D-alanine as substrate and with free CC enzyme (at 25 degrees Celsius and at pH 8) (PubMed:18343336). kcat is CC 23.3 sec(-1) with D-alanine as substrate and with immobilized enzyme CC (at 25 degrees Celsius and at pH 8) (PubMed:18343336). kcat is 83 CC sec(-1) with D-alanine as substrate (at 25 degrees Celsius and at pH CC 8.5) (PubMed:12021281). kcat is 81 sec(-1) with D-alanine as CC substrate (at 25 degrees Celsius and at pH 8.5) (PubMed:17145127). CC kcat is 330 sec(-1) with D-alanine as substrate and with free enzyme CC (at 15 degrees Celsius and at pH 8.5) (PubMed:19694805). kcat is 81.3 CC sec(-1) with D-alanine as substrate (at 25 degrees Celsius and at pH CC 8.5) (PubMed:15058991). kcat is 77.3 sec(-1) with D-proline as CC substrate (at 25 degrees Celsius and at pH 8.5) (PubMed:12021281). CC kcat is 21.6 sec(-1) with D-asparagine as substrate (at 25 degrees CC Celsius and at pH 8.5) (PubMed:12021281). kcat is 18.9 sec(-1) with CC D-glutamine as substrate (at 25 degrees Celsius and at pH 8.5) CC (PubMed:12021281). kcat is 76 sec(-1) with D-methionine as substrate CC (at 25 degrees Celsius and at pH 8.5) (PubMed:12021281). kcat is 20 CC sec(-1) with D-arginine as substrate (at 25 degrees Celsius and at pH CC 8.5) (PubMed:17145127). kcat is 0.5 sec(-1) with D-aspartate as CC substrate (at 25 degrees Celsius and at pH 8.5) (PubMed:12021281, CC PubMed:17145127). kcat is 1 sec(-1) with D-glutamate as substrate (at CC 25 degrees Celsius and at pH 8.5) (PubMed:12021281). kcat is 72 CC sec(-1) with cephalosporin C (CPC) as substrate (at 25 degrees CC Celsius and at pH 8.5) (PubMed:17145127). kcat is 73.3 sec(-1) with CC cephalosporin C (CPC) as substrate (at 25 degrees Celsius and at pH CC 8.5) (PubMed:15058991). {ECO:0000269|PubMed:12021281, CC ECO:0000269|PubMed:15058991, ECO:0000269|PubMed:17145127, CC ECO:0000269|PubMed:18343336, ECO:0000269|PubMed:19694805}; CC pH dependence: CC Optimum pH is 8-10. {ECO:0000269|PubMed:15058991, CC ECO:0000269|PubMed:18343336}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius. CC {ECO:0000269|PubMed:18343336}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12021281, CC ECO:0000269|PubMed:12208501, ECO:0000269|PubMed:12445787, CC ECO:0000269|PubMed:15310841}. CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:1680680}. CC -!- INDUCTION: Induced by D-alanine. {ECO:0000269|PubMed:12961754, CC ECO:0000269|PubMed:1680680}. CC -!- BIOTECHNOLOGY: Capable of converting cephalosporin C (CPC) into 7-beta- CC (5-carboxy-5-oxopentanamido)-cephalosporinic acid, an initial material CC of different beta-lactam antibiotics (PubMed:17145127, PubMed:7654197, CC PubMed:9383984). Has been used as a biosensor to detect and quantify D- CC amino acids; when the technology was implanted in the cortex of rats, CC the increase in the concentration of D-serine following an CC intraperitoneal injection could be sensed (PubMed:18229946). Has been CC used to resolve racemic mixtures of D,L-amino acids to yield CC enantiomerically pure isomers for pharmacological and peptide research CC uses (Ref.14). Has potential uses in anticancer treatment strategies; a CC recombinant enzyme with improved activity at low oxygen and substrate CC concentrations is targeted to tumor cells where it oxidizes D-amino CC acid prodrugs, yielding the cytotoxic metabolite hydrogen peroxide CC (PubMed:19694805, PubMed:34174417, PubMed:9472778). CC {ECO:0000269|PubMed:17145127, ECO:0000269|PubMed:18229946, CC ECO:0000269|PubMed:19694805, ECO:0000269|PubMed:34174417, CC ECO:0000269|PubMed:7654197, ECO:0000269|PubMed:9383984, CC ECO:0000269|PubMed:9472778, ECO:0000269|Ref.14}. CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}. 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; U60066; AAB51107.1; -; mRNA. DR EMBL; Z71657; CAA96323.1; -; Genomic_DNA. DR EMBL; AF003339; AAB93974.1; -; mRNA. DR EMBL; AF003340; AAB93975.1; -; Genomic_DNA. DR PDB; 1C0I; X-ray; 1.90 A; A=1-361. DR PDB; 1C0K; X-ray; 1.46 A; A=1-361. DR PDB; 1C0L; X-ray; 1.73 A; A=1-361. DR PDB; 1C0P; X-ray; 1.20 A; A=1-361. DR AlphaFoldDB; P80324; -. DR SMR; P80324; -. DR OrthoDB; 2015447at2759; -. DR BRENDA; 1.4.3.3; 5424. DR SABIO-RK; P80324; -. DR EvolutionaryTrace; P80324; -. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB. DR GO; GO:0003884; F:D-amino-acid oxidase activity; IDA:UniProtKB. DR GO; GO:0047821; F:D-glutamate oxidase activity; EXP:UniProtKB. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0043799; F:glycine oxidase activity; EXP:UniProtKB. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:TreeGrafter. DR GO; GO:0046416; P:D-amino acid metabolic process; IDA:UniProtKB. DR GO; GO:0019740; P:nitrogen utilization; ISS:UniProtKB. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR006181; D-amino_acid_oxidase_CS. DR InterPro; IPR023209; DAO. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1. DR PANTHER; PTHR11530:SF30; FAD DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01266; DAO; 1. DR PIRSF; PIRSF000189; D-aa_oxidase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 1. DR PROSITE; PS00677; DAO; 1. DR PDBsum; 1C0I; -. DR PDBsum; 1C0K; -. DR PDBsum; 1C0L; -. DR PDBsum; 1C0P; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; KW Oxidoreductase; Peroxisome; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..368 FT /note="D-amino-acid oxidase" FT /id="PRO_0000162767" FT REGION 308..321 FT /note="Required for dimerization" FT /evidence="ECO:0000269|PubMed:12208501" FT MOTIF 366..368 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT BINDING 12 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 15 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 35 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 36 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 47 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 48 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 54 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 58 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12445787, FT ECO:0007744|PDB:1C0I" FT BINDING 162 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 223 FT /ligand="(R)-lactate" FT /ligand_id="ChEBI:CHEBI:16004" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0007744|PDB:1C0K" FT BINDING 223 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12445787, FT ECO:0007744|PDB:1C0I" FT BINDING 238 FT /ligand="(R)-lactate" FT /ligand_id="ChEBI:CHEBI:16004" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0007744|PDB:1C0K" FT BINDING 238 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12445787, FT ECO:0007744|PDB:1C0I" FT BINDING 285 FT /ligand="(R)-lactate" FT /ligand_id="ChEBI:CHEBI:16004" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0007744|PDB:1C0K" FT BINDING 285 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12445787, FT ECO:0007744|PDB:1C0I" FT BINDING 285 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 334 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 335 FT /ligand="(R)-lactate" FT /ligand_id="ChEBI:CHEBI:16004" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0007744|PDB:1C0K" FT BINDING 335 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12445787, FT ECO:0007744|PDB:1C0I" FT BINDING 335 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 337 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0L, ECO:0007744|PDB:1C0P" FT BINDING 338 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT BINDING 339 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:11070076, FT ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, FT ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, FT ECO:0007744|PDB:1C0P" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT MUTAGEN 19 FT /note="S->G: Increases activity at low oxygen and D-alanine FT concentrations; when associated with P-120; R-144; M-321 FT and V-345." FT /evidence="ECO:0000269|PubMed:19694805" FT MUTAGEN 60 FT /note="T->A: Increases activity on D-arginine; when FT associated with R-144 and E-152." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 118 FT /note="L->H: Increases activity on D-arginine." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 120 FT /note="S->P: Increases activity at low oxygen and D-alanine FT concentrations; when associated with G-19; R-144; M-321 and FT V-345." FT /evidence="ECO:0000269|PubMed:19694805" FT MUTAGEN 144 FT /note="Q->R: Increases activity on D-aspartate. Increases FT activity at low oxygen and D-alanine concentrations. FT Increases activity on D-alanine; when associated with FT D-199; C-223 and R-329 or when associated with G-19; P-120; FT M-321 and V-345. Increases activity on D-arginine; when FT associated with A-60 and E-152." FT /evidence="ECO:0000269|PubMed:15310841, FT ECO:0000269|PubMed:19694805, ECO:0000269|PubMed:34174417" FT MUTAGEN 152 FT /note="K->E: Increases activity on D-arginine; when FT associated with A-60 and R-144." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 199 FT /note="G->D: Increases activity on D-alanine; when FT associated with R-144; D-199; C-223 and R-329." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 213 FT /note="M->E: Alters substrate specificity; capable of FT oxidizing D-amino acids with an acidic side-chain. FT Increases activity on D-aspartate." FT /evidence="ECO:0000269|PubMed:17145127" FT MUTAGEN 213 FT /note="M->G,R: Alters substrate specificity." FT /evidence="ECO:0000269|PubMed:12021281, FT ECO:0000269|PubMed:15310841, ECO:0000269|Ref.14" FT MUTAGEN 213 FT /note="M->R: Capable of oxidizing D-amino acids with an FT acidic side-chain and increases activity on D-aspartate." FT /evidence="ECO:0000269|PubMed:12021281, FT ECO:0000269|PubMed:15310841" FT MUTAGEN 223 FT /note="Y->C: Increases activity on D-alanine; when FT associated with R-144; D-199 and R-329." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 223 FT /note="Y->F,S: Decreases activity." FT /evidence="ECO:0000269|PubMed:17145127" FT MUTAGEN 238 FT /note="Y->F,S: Decreases activity." FT /evidence="ECO:0000269|PubMed:17145127" FT MUTAGEN 238 FT /note="Y->R: Alters substrate specificity; capable of FT oxidizing D-amino acids with an acidic side-chain. FT Increases activity on D-aspartate." FT /evidence="ECO:0000269|PubMed:17145127" FT MUTAGEN 242 FT /note="D->V: Increases activity on D-arginine; when FT associated with R-253 and V-304." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 253 FT /note="Q->R: Increases activity on D-arginine; when FT associated with V-242 and V-304." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 304 FT /note="D->V: Increases activity on D-arginine; when FT associated with V-242 and R-253." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 308..321 FT /note="Missing: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:12208501" FT MUTAGEN 321 FT /note="K->M: Increases activity at low oxygen and D-alanine FT concentrations; when associated with G-19; P-120; R-144 and FT V-345." FT /evidence="ECO:0000269|PubMed:19694805" FT MUTAGEN 329 FT /note="H->R: Increases activity on D-alanine; when FT associated with R-144; D-199 and C-223." FT /evidence="ECO:0000269|PubMed:15310841" FT MUTAGEN 335 FT /note="S->G,R: Decreases activity." FT /evidence="ECO:0000269|PubMed:17145127" FT MUTAGEN 339 FT /note="Q->E,N: Decreases activity." FT /evidence="ECO:0000269|PubMed:17145127" FT MUTAGEN 345 FT /note="A->V: Increases activity at low oxygen and D-alanine FT concentrations; when associated with G-19; P-120; R-144 and FT M-321." FT /evidence="ECO:0000269|PubMed:19694805" FT STRAND 6..10 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 14..25 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 29..36 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1C0P" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 65..81 FT /evidence="ECO:0007829|PDB:1C0P" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 86..99 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 100..106 FT /evidence="ECO:0007829|PDB:1C0P" FT TURN 107..111 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:1C0L" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 128..136 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 139..152 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 194..205 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:1C0P" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 249..262 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 276..288 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 293..302 FT /evidence="ECO:0007829|PDB:1C0P" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:1C0P" FT STRAND 323..331 FT /evidence="ECO:0007829|PDB:1C0P" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:1C0L" FT HELIX 337..359 FT /evidence="ECO:0007829|PDB:1C0P" SQ SEQUENCE 368 AA; 40076 MW; 99940118BCFA886E CRC64; MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW AGANWTPFMT LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE DGLLGHWYKD ITPNYRPLPS SECPPGAIGV TYDTLSVHAP KYCQYLAREL QKLGATFERR TVTSLEQAFD GADLVVNATG LGAKSIAGID DQAAEPIRGQ TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV GDWDLSVNPE TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ LVDEAFQRYH GAARESKL //