Detail Information for IndEnz0018000378
IED ID IndEnz0018000378
Enzyme Type ID peroxidase000378
Protein Name Dual oxidase 1
DUOX1
EC 1.11.1.-
EC 1.6.3.1
Blistered cuticle protein 3
NADPH thyroid oxidase 1
Gene Name bli-3 F56C11.1
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MRSKHVLYIAILFSSIFGGKGIQQNEEFQRYDGWYNNLANSEWGSAGSRLHRDARSYYSDGVYSVNNSLPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQSNGVSCPLETLKIQVPLCDNVFDKECEGKTEIPFTRAKYDKATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSSLRSFKQGRLAEGVPGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIHREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVRLSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNKCEFRTEVGGYPALRLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGLAPKTWETMNEDFYKKHTAKVEKLKELYGGNILYLDAYVGGMLEGGENGPGELFKEIIKDQFTRIRDGDRFWFENKLNGLFTDEEVQMIHSITLRDIIKATTDIDETMLQKDVFFFKEGDPCPQPFQVNTTGLEPCVPFMQSTYWTDNDTTYVFTLIGLACVPLICYGIGRYLVNRRIAIGHNSACDSLTTDFANDDCGAKGDIYGVNALEWLQEEYIRQVRIEIENTTLAVKKPRGGILRKIRFETGQKIELFHSMPNPSAMHGPFVLLSQKNNHHLVIRLSSDRDLSKFLDQIRQAASGINAEVIIKDEENSILLSQAITKERRQDRLDLFFREAYAKAFNDSELQDSETSFDSSNDDILNETISREELASAMGMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVLREFVNAPQKQKLQTLFKMCDLEGKNKVLRKDLAELVKSLNQTAGVHITESVQLRLFNEVLHYAGVSNDAKYLTYDDFNALFSDIPDKQPVGLPFNRKNYQPSIGETSSLNSFAVVDRSINSSAPLTLIHKVSAFLETYRQHVFIVFCFVAINLVLFFERFWHYRYMAENRDLRRVMGAGIAITRGAAGALSFCMALILLTVCRNIITLLRETVIAQYIPFDSAIAFHKIVALFAAFWATLHTVGHCVNFYHVGTQSQEGLACLFQEAFFGSNFLPSISYWFFSTITGLTGIALVAVMCIIYVFALPCFIKRAYHAFRLTHLLNIAFYALTLLHGLPKLLDSPKFGYYVVGPIVLFVIDRIIGLMQYYKKLEIVNAEILPSDIIYIEYRRPREFKYKSGQWVTVSSPSISCTFNESHAFSIASSPQDENMKLYIKAVGPWTWKLRSELIRSLNTGSPFPLIHMKGPYGDGNQEWMDYEVAIMVGAGIGVTPYASTLVDLVQRTSSDSFHRVRCRKVYFLWVCSTHKNYEWFVDVLKNVEDQARSGILETHIFVTQTFHKFDLRTTMLYICEKHFRATNSGISMFTGLHAKNHFGRPNFKAFFQFIQSEHKEQSKIGVFSCGPVNLNESIAEGCADANRQRDAPSFAHRFETF
Enzyme Length 1497
Uniprot Accession Number O61213
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Peroxidase activity is inhibited by aminobenzohydrazide. {ECO:0000269|PubMed:11514595}.
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:11514595}; 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:11514595};
DNA Binding
EC Number 1.11.1.-; 1.6.3.1
Enzyme Function FUNCTION: Plays a role in cuticle biogenesis (PubMed:11514595, PubMed:19406744, PubMed:23028364, PubMed:25480962, PubMed:18460651). In complex with doxa-1 and tsp-15, produces reactive oxygen species (ROS), which are probably used by mlt-7 for tyrosine cross-linking, thus stabilizing cuticular extracellular matrix (PubMed:11514595, PubMed:19406744, PubMed:23028364). May regulate the production of ROS by playing a role in modulating proline catabolism (PubMed:27974198). Required in combination with mlt-7 for correct formation of cross-links in cuticle collagens (PubMed:19406744). Association with the GTPase rho-1 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity (PubMed:28085666). {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:18460651, ECO:0000269|PubMed:19406744, ECO:0000269|PubMed:23028364, ECO:0000269|PubMed:25480962, ECO:0000269|PubMed:27974198, ECO:0000269|PubMed:28085666}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (4); Glycosylation (4); Mutagenesis (3); Region (1); Sequence conflict (2); Signal peptide (1); Topological domain (8); Transmembrane (7)
Keywords Calcium;FAD;Flavoprotein;Glycoprotein;Hydrogen peroxide;Membrane;NADP;Oxidoreductase;Peroxidase;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 11099033; 11231151; 12619137; 14551910; 15084750; 15489339; 16122351; 17164286; 19165329; 19343510; 19460756; 19502579; 19687201; 20439774; 20439776; 20865164; 20947510; 21085631; 21177967; 21367940; 22216003; 22267497; 22347378; 2245913; 22560298; 22634595; 23800452; 24884423; 25487147; 25909649; 27540856; 29348603; 30166349; 30695063; 4366476; 6593563;
Motif
Gene Encoded By
Mass 170,416
Kinetics
Metal Binding
Rhea ID RHEA:11264; RHEA:11260
Cross Reference Brenda 1.6.3.1;