Detail Information for IndEnz0018000372
IED ID IndEnz0018000372
Enzyme Type ID peroxidase000372
Protein Name Dual oxidase
EC 1.11.1.-
EC 1.6.3.1
Gene Name Duox CG3131
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MSVPSAPHQRAESKNRVPRPGQKNRKLPKLRLHWPGATYGGALLLLLISYGLELGSVHCYEKMYSQTEKQRYDGWYNNLAHPDWGSVDSHLVRKAPPSYSDGVYAMAGANRPSTRRLSRLFMRGKDGLGSKFNRTALLAFFGQLVANEIVMASESGCPIEMHRIEIEKCDEMYDRECRGDKYIPFHRAAYDRDTGQSPNAPREQINQMTAWIDGSFIYSTSEAWLNAMRSFHNGTLLTEKDGKLPVRNTMRVPLFNNPVPSVMKMLSPERLFLLGDPRTNQNPAILSFAILFLRWHNTLAQRIKRVHPDWSDEDIYQRARHTVIASLQNVIVYEYLPAFLGTSLPPYEGYKQDIHPGIGHIFQAAAFRFGHTMIPPGIYRRDGQCNFKETPMGYPAVRLCSTWWDSSGFFADTSVEEVLMGLASQISEREDPVLCSDVRDKLFGPMEFTRRDLGALNIMRGRDNGLPDYNTARESYGLKRHKTWTDINPPLFETQPELLDMLKEAYDNKLDDVDVYVGGMLESYGQPGEFFTAVIKEQFQRLRDADRFWFENERNGIFTPEEIAELRKITLWDIIVNSTDVKEEEIQKDVFMWRTGDPCPQPMQLNATELEPCTYLEGYDYFSGSELMFIYVCVFLGFVPILCAGAGYCVVKLQNSKRRRLKIRQEALRAPQHKGSVDKMLAREWLHANHKRLVTVKFGPEAAIYTVDRKGEKLRTFSLKHIDVVSVEESATNHIKKKPYILLRVPSDHDLVLELESYGARRKFVKKLEDFLLLHKKEMTLMEVNRDIMLARAETRERRQKRLEYFFREAYALTFGLRPGERRRRSDASSDGEVMTVMRTSLSKAEFAAALGMKPNDMFVRKMFNIVDKDQDGRISFQEFLETVVLFSRGKTDDKLRIIFDMCDNDRNGVIDKGELSEMMRSLVEIARTTSLGDDQVTELIDGMFQDVGLEHKNHLTYQDFKLMMKEYKGDFVAIGLDCKGAKQNFLDTSTNVARMTSFNIEPMQDKPRHWLLAKWDAYITFLEENRQNIFYLFLFYVVTIVLFVERFIHYSFMAEHTDLRHIMGVGIAITRGSAASLSFCYSLLLLTMSRNLITKLKEFPIQQYIPLDSHIQFHKIAACTALFFSVLHTVGHIVNFYHVSTQSHENLRCLTREVHFASDYKPDITFWLFQTVTGTTGVMLFIIMCIIFVFAHPTIRKKAYNFFWNMHTLYIGLYLLSLIHGLARLTGPPRFWMFFLGPGIVYTLDKIVSLRTKYMALDVIDTDLLPSDVIKIKFYRPPNLKYLSGQWVRLSCTAFRPHEMHSFTLTSAPHENFLSCHIKAQGPWTWKLRNYFDPCNYNPEDQPKIRIEGPFGGGNQDWYKFEVAVMVGGGIGVTPYASILNDLVFGTSTNRYSGVACKKVYFLWICPSHKHFEWFIDVLRDVEKKDVTNVLEIHIFITQFFHKFDLRTTMLYICENHFQRLSKTSIFTGLKAVNHFGRPDMSSFLKFVQKKHSYVSKIGVFSCGPRPLTKSVMSACDEVNKTRKLPYFIHHFENFG
Enzyme Length 1537
Uniprot Accession Number Q9VQH2
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Peroxidase activity is inhibited by aminotriazole and azide. {ECO:0000269|PubMed:16272120}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1; Evidence={ECO:0000269|PubMed:16272120}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; Evidence={ECO:0000269|PubMed:16272120};
DNA Binding
EC Number 1.11.1.-; 1.6.3.1
Enzyme Function FUNCTION: Plays a role in innate immunity limiting microbial proliferation in the gut (PubMed:16272120, PubMed:25639794). Acts downstream of a hh-signaling pathway to induce the production of reactive oxygen species (ROS) in response to intestinal bacterial infection (PubMed:25639794). May generate antimicrobial oxidative burst through its peroxidase-like domain (PubMed:16272120). {ECO:0000269|PubMed:16272120, ECO:0000269|PubMed:25639794}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (5); Erroneous termination (1); Frameshift (1); Glycosylation (4); Metal binding (9); Modified residue (2); Region (2); Topological domain (8); Transmembrane (7)
Keywords Calcium;FAD;Flavoprotein;Glycoprotein;Hydrogen peroxide;Membrane;Metal-binding;NADP;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Modified Residue MOD_RES 826; /note=Phosphoserine; /evidence=ECO:0000250; MOD_RES 1105; /note=Phosphotyrosine; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 1039909; 14778558; 15020472; 15204079; 16858400; 17216353; 17246014; 17247021; 18039034; 18419806; 19289084; 19317464; 19668222; 19797770; 19958789; 20188558; 20220848; 20371351; 21074052; 21399827; 21808060; 21979942; 22242003; 22368770; 22520468; 22724070; 22817988; 22858408; 22952763; 23071443; 23394834; 23663779; 23685204; 23781070; 23808845; 23944235; 24127584; 24141879; 24380076; 24381562; 24409421; 24439372; 24455491; 24673174; 24735869; 24799191; 24819984; 24856462; 24983497; 24997434; 25254641; 25421701; 25687947; 25688716; 25945494; 26068126; 26136621; 26353752; 26431326; 26443856; 26587980; 26634780; 26655037; 26690827; 26726767; 26876781; 26878754; 26898463; 26935105; 27160597; 27262554; 27274436; 27562340; 27575697; 27923120; 28069988; 28248301; 28289197; 28462587; 28753614; 28760809; 28853394; 29049360; 29091025; 29420191; 29503179; 29540218; 29644870; 29707694; 29750169; 29752064; 29787709; 29795158; 29849035; 29952680; 30166445; 30180210; 30325949; 30353950; 30356215; 30385770; 30446385; 30540251; 30587065; 30733377; 30770378; 30822306; 30926832; 30986429; 31009489; 31068592; 31315941; 31316388; 31554796; 31575764; 31610128; 31698828; 32075729; 32078802; 32228858; 32277031; 32339931; 32561812; 32612612; 32686670; 32791328; 32917927; 33050786; 33176146; 33187802; 33400912; 33600942; 33863891; 33972730; 34126772; 34290589; 34445633; 34600048; 34622778; 4255937; 4624174; 6804094; 7707961; 8001779; 8100740; 826447; 8458732; 8782435; 9409834;
Motif
Gene Encoded By
Mass 177,690
Kinetics
Metal Binding METAL 868; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 870; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 872; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 874; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 879; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 904; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 906; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 908; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 915; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448
Rhea ID RHEA:11264; RHEA:11260
Cross Reference Brenda