IED ID | IndEnz0018000706 |
Enzyme Type ID | peroxidase000706 |
Protein Name |
Peroxidase DmPO EC 1.11.1.7 Chorion peroxidase |
Gene Name | Pxd HDC14047 PO CG3477 |
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 | MIRARDLLLLALLGFISSALGLKVSSGYHIVHNQPQSSFPNYHGFSYLQGSAPYVIGNSLPTSPAPQNPFSSPASPPVSAYGYSFPTAGRVSCAAPPAVCEKTAYRTLDGSCNHLEQPGLGVANSKYGRLLTPKYADGISAPTRSVTGDELPSARLVSLVAFGEQDVPDPEFTLHNMQWGQIMTHDMSMQAGGTQSKKHPTRCCTDDGRLIGLDTAHKTCFAIIVPPHDPAYSQVGTECLNFVRTLTDRDSNCQYQGGPAEQLTVVTSYLDLSLVYGNSIQQNSDIREFQGGRMIVEERNGAKWLPLSRNVTGDCDAVDASEVCYRSGDVRVNQNPGLAILQTILLREHNRIADALSALNPHYDDRTLFQEARKINIAQYQQISYYEWLPIFLGGENMLKNRLIYKAPSGSYINDFDPNIDPSVLNEHATAAFRYFHSQIEGRLDLLSELRQVLGSLTLSDWFNRPGIIEVGDNFDSLTRGHATQPEELTDINFDRQIKHFLFRRNMPFGSDLRSLDIQRNRDHGLASYNDMREFCGLRRAHSWEGYGDLISPPILEKLKSLYPSHEDVDLTVGASLEAHVAGALAGPTFLCILTEQFYRTRVGDRFFFENGDKLTGFTPDQLEELRKASMARLLCDNGNHISSMQPEAFRTVSHSNPIIPCSNIPQVDLTKWIDQKLYATVDPSHYGKK |
Enzyme Length | 690 |
Uniprot Accession Number | Q01603 |
Absorption | |
Active Site | ACT_SITE 185; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; |
DNA Binding | |
EC Number | 1.11.1.7 |
Enzyme Function | FUNCTION: Involved in the chorion hardening process, through protein cross-linking mediated by the formation of di- and tri-tyrosine bonds. {ECO:0000269|PubMed:15979004}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (4); Erroneous initiation (1); Glycosylation (1); Metal binding (1); Sequence conflict (4); Signal peptide (1); Site (1) |
Keywords | Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11157786; 12459925; 15668397; 16336044; 19216785; 20015541; 20220848; 21074052; 22952763; 23071443; 25294943; 25312911; 25387828; 26353752; 26551273; 26568309; 26587980; 27274984; 27357258; 27794539; 9545464; |
Motif | |
Gene Encoded By | |
Mass | 76,719 |
Kinetics | |
Metal Binding | METAL 437; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |