Detail Information for IndEnz0016000126
IED ID IndEnz0016000126
Enzyme Type ID tyrosinase000126
Protein Name Phenoloxidase 1
EC 1.14.18.-
Prophenoloxidase-I
Gene Name PPO1 proPO-I
Organism Holotrichia diomphalia (Korean black chafer)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Coleoptera Polyphaga Scarabaeiformia Scarabaeoidea Scarabaeidae (scarab beetles) Melolonthinae (May beetles & June bugs) Holotrichia Holotrichia diomphalia (Korean black chafer)
Enzyme Sequence MSDKNKLLLLFDRPLETVIVPRGPDQEAFDVPVDLLSDRYKAIGVQVSNRFGEETKSKIPVKKISPPPLGEILDLPRQANFSLFIPKHRKIAGRLINIFLGMKDTDDLQSMAIFARERVNPYLFNYCFSVAILHRPDTQDLDIPSFIQTFPDKYLDSQVFSRAREEATLVPEGQRVPIEIPRDYTASDLEVEHRVAYFREDLGINLHHWHWHLVYPFEGAEQVVRKDRRGELFYYMHQQVIARYNLERFCNALKRVTRFTEWKDPIPEAYFPKLDSLVASRAWPARVTDQKLSNLRRDQDQITQDVDDLYRWRDRIYEAIHSGFVQTDGGGRQELTEFGGIDILGNIVESSNLSVNRTLYGDLHNMGHVFISYIHDPDHRHLETFGVMGDSATAMRDPVFYRWHAYIDDLFQQFKGSLPRYTEEQLNYPGITVTGVSVQSQGGAANTLNTFWQQSDVDMSRGMDFQPRGSVFARFTHLNHQPFAYNITVNNASGGNKRGTCRIFLGPKTDERRTAWLFKDQRLLFIELDRFVVNLRQGENTITRNSTESSVTIPFERTFRNLDLSRPVGGEALAQFNFCGCGWPQHMLIPKGTPEGYDCQLFVMISNFDDDQVVQSTEGICNDAMSYCGIKDRLYPDKRSMGYPFDRLPRNNVNTLQEFLTPNMRVQDCVIKFTDRVVVPRPRN
Enzyme Length 684
Uniprot Accession Number Q8I6K1
Absorption
Active Site ACT_SITE 349; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q8MZM3
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 1.14.18.-
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 oxidation of o-diphenols (N-acetyldopamine, 4-methylcatechol and dopamine). Cannot oxidize monophenols and p-phenols (L-tyrosine, tyramine, gentisic acid and hydroquinone). Binds to the surface of hemocytes and is involved in hemocyte melanization. Activation of the enzyme in response to bacterial lipopolysaccharides (LPS) suggests it may play a role in innate immunity. {ECO:0000250|UniProtKB:O44249, ECO:0000250|UniProtKB:Q8I6K2}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (2); Glycosylation (6); Metal binding (6); Propeptide (1)
Keywords Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunity;Innate immunity;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Secreted;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9085271}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:9085271}.
Modified Residue
Post Translational Modification PTM: Propeptide cleaved by PPAF1. {ECO:0000269|PubMed:12185078}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 79,073
Kinetics
Metal Binding METAL 208; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 212; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 237; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 364; /note=Copper B; /evidence=ECO:0000250|UniProtKB:O44249; METAL 368; /note=Copper B; /evidence=ECO:0000250|UniProtKB:O44249; METAL 404; /note=Copper B; /evidence=ECO:0000250|UniProtKB:O44249
Rhea ID
Cross Reference Brenda