| IED ID | IndEnz0002008068 |
| Enzyme Type ID | protease008068 |
| Protein Name |
Phenoloxidase 3 EC 1.14.18.1 Diphenoloxidase subunit A3 Tyrosinase A3 |
| Gene Name | PPO3 Dox-A3 proPO59 GG22822 |
| Organism | Drosophila erecta (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 erecta (Fruit fly) |
| Enzyme Sequence | MADKKNLLLLFDHPTEPVFMDKGGNGTVFDVPASYVTDRYNKMCKKVQRRVSGGFEKNVLVKEIPIPDLSCSMRLGRSEQFSLFLESHRQMACHLIDVFIKMPTVDELQSVAVYARDRVNPVLFNYALSVAMLHRSDTKDLGLPAFAQIFPDRFIDSQMLRTMREESFVVERSAARLPVHSSVKYTASDLDVEHRLWYFREDLGVNLHHWHWHLVYPNTAPDRSIVDKDRRGELFYYMHQQIIARYNAERLCNHMARVQPFNNLEEPIAEGYFPKMDSLVASRAFPPRFDNTRLSDVDRPINQLRVGIDDMKRWRERIYEAIHQGYVLDANHKKIVLDDVKGIDILGNIIESSQLTPNKTLYGDLHNKGHILIAFSHDPTNKHLEYAGVMGDASTAMRDPIFYKWHAFIDNLFQEHKRQLSPYTEEDLTFPDVRVQSIQVESQGQVNRLTTFWQESDVDMSRGLDFVPRGHVLARFTHLQHHPFSYTIEVENSSEATRYGYVRIFLAPKLDDGNATMLLEQQRRMMVELDKFVVTMPPGSHTITRDSTESSVTIPFKRTFRNMDNPGEPQNFLCGCGWPQHMLIPKGRAEGLSFELFVMVSNYEDDKVDQKPEDCECSIAASYCGLRDRLYPDRKSMGFPFDRQPRSGSELLEKFLTPNMCSIEVIISHEARTEKIPELPDHS |
| Enzyme Length | 683 |
| Uniprot Accession Number | Q8I1F6 |
| Absorption | |
| Active Site | ACT_SITE 351; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q8MZM3 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1; |
| DNA Binding | |
| EC Number | 1.14.18.1 |
| Enzyme Function | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (6); Propeptide (1); Sequence conflict (3) |
| Keywords | Cleavage on pair of basic residues;Copper;Disulfide bond;Glycoprotein;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Secreted;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q27451}. |
| Modified Residue | |
| Post Translational Modification | PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 79,020 |
| Kinetics | |
| Metal Binding | METAL 209; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q27451; METAL 213; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q27451; METAL 239; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q27451; METAL 366; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q27451; METAL 370; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q27451; METAL 406; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q27451 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda |