| IED ID | IndEnz0016000118 |
| Enzyme Type ID | tyrosinase000118 |
| Protein Name |
Phenoloxidase subunit 1 EC 1.14.18.1 proPO-P1 |
| Gene Name | |
| Organism | Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Sphingidae (hawkmoths) Sphinginae (small-eyed sphinx moth) Sphingini Manduca Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) |
| Enzyme Sequence | MTDAKNNLLYFFDRPNEPCFMQKGEDKVVFEIPDHYYPDKYKSLSNTLSNRFGNEATKRIPIRNITLPNLEVPMQLPYNDQFSLFVPKHRTMAAKLIDIFMGMRDVEDLQSVCSYCQLRINPYMFNYCLSVAILHRPDTKGLSIPTFAETFPDKFMDSKVFLRAREVSNVVISGSRMPVNVPINYTANTTEPEQRVAYFREDIGINLHHWHWHLVYPFDSADRSIVNKDRRGELFYYMHQQIIGRYNVERMCNGLPQVKPFSDFSAPIEEGYFPKLDSQVASRTWPPRFAGSVFRNLDRTVDQVKIDVRKLFTWRDQFLEAIQKMAIKMPNGRELPLDEVTGIDMLGNLMESSIISPNRGYYGDLHNMGHVFAAYTHDPDHRHLEQFGVMGDSATAMRDPFFYRWHRFVDDVFNIYKEKLTPYTNERLDFPGVRVSSVGIEGARPNTLRTLWQQSTVELGRGLDFTPRGSVLARFTHLQHDEFQYVIEVNNTTGGNLMGTVRIFMAPKVDDNGQPMSFNKQRRLMIELDKFSQALRPGTNTIRRRSVDSSVTIPYERTFRNQSERPGDPGTAGAAEFDFCGCGWPHHMLIPKGTAQGYPVVLFVMISNWNNDRIEQDLVGSCNDAASYCGIRDRKYPDKQAMGYPFDRKMANDAATLSDFLRPNMAVRDCSIQFSDTTVERGQQG |
| Enzyme Length | 685 |
| Uniprot Accession Number | O44249 |
| Absorption | |
| Active Site | ACT_SITE 351; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q8MZM3 |
| Activity Regulation | ACTIVITY REGULATION: Activated by immulectin and lipopolysaccharide. {ECO:0000269|PubMed:10436935}. |
| 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. Binds to the surface of hemocytes and is involved in hemocyte melanization. {ECO:0000269|PubMed:16291091, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (19); Chain (1); Disulfide bond (2); Helix (35); Initiator methionine (1); Metal binding (6); Turn (7) |
| Keywords | 3D-structure;Copper;Disulfide bond;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9474780}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9474780}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3HHS; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,966 |
| Kinetics | |
| Metal Binding | METAL 209; /note=Copper A; /evidence=ECO:0000269|PubMed:19805072; METAL 213; /note=Copper A; /evidence=ECO:0000269|PubMed:19805072; METAL 239; /note=Copper A; /evidence=ECO:0000269|PubMed:19805072; METAL 366; /note=Copper B; /evidence=ECO:0000269|PubMed:19805072; METAL 370; /note=Copper B; /evidence=ECO:0000269|PubMed:19805072; METAL 406; /note=Copper B; /evidence=ECO:0000269|PubMed:19805072 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda |