| IED ID | IndEnz0016000152 |
| Enzyme Type ID | tyrosinase000152 |
| Protein Name |
Phenoloxidase subunit 2 EC 1.14.18.1 Prophenoloxidase subunit 2 |
| Gene Name | |
| Organism | Galleria mellonella (Greater wax moth) |
| 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 Pyraloidea Pyralidae (snout moths) Galleriinae Galleria Galleria mellonella (Greater wax moth) |
| Enzyme Sequence | MTDRVKSLQLLFDRPNEPLITPKGENGAIFQLTQDLLPVDYEDNGIALNNRFGEEADEKIPLKPLSNPPQFPIASQLPTDADFSLFLPRHQEMATEVIDVLMNIPENQLDDLLSSCVYARGRLNPQLFNYCYSVVLMHRRDTRNVPIQNFAETFPSKFLDSQAFAQARETAAVFPRGIPRTPIIIPRDYTATDLEEEHRLAYWREDIGINLHHWQWHLVYPFTASDRSIVAKDRRGELFFYMHQQIIARYNCERINNSLKRVKKFNNWREPIPEAYFPKLDSLTSSRGWPPRQANMTWQDLNRPVDGLNVTISDMERWRRNLEEAVSMGTVTLPDGSTRPLDIDTLGNMVEASILSPNRELYGSVHNNGHSFSAYVHDPSHRYLENFGVIADEATTMRDPFFYRWHAWVDDLFQKHKESNFVRPYSRSELENPGVQVTSVSVETQGSPQNVLSTFWMSSDVDLSRGLDFSNRGPVYARFTHLNHRPFRYVIKVNNSGNARRTTVRIFISPKFDERNLAWSLVDQRKMFIEMDRFVTPLKAGENTITRQSTESTFTIPFEQTFRDLSVQADDPRRVDLAAFNFCGCGWPQHMLVPKGTEAGAPYVFFVMLSNYDLDRIDEPGNSPEISCKEASSFCGLRDRKYPDKRAMGFPFDRPSRTATSIEDFILPNMALQDITIRLNNVVEANPRNPRT |
| Enzyme Length | 692 |
| Uniprot Accession Number | Q6UEH6 |
| 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=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; Evidence={ECO:0000250|UniProtKB:C0HJM0}; 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; Evidence={ECO:0000250|UniProtKB:C0HJM0}; |
| DNA Binding | |
| EC Number | 1.14.18.1 |
| Enzyme Function | FUNCTION: Copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (By similarity). 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). Binds to the surface of hemocytes and is involved in hemocyte melanization (By similarity). Binds the A.niger cell wall component alpha-1,3-glucan, a fungal pathogen-associated molecular pattern (PAMP) that activates the host immune response (PubMed:34443685). {ECO:0000250|UniProtKB:Q25519, ECO:0000269|PubMed:34443685}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (6); Propeptide (1) |
| Keywords | Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34443685}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:34443685}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 79,842 |
| Kinetics | |
| Metal Binding | METAL 213; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 217; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 243; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 366; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 370; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 406; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q25519 |
| Rhea ID | RHEA:18117; RHEA:34287 |
| Cross Reference Brenda |