| IED ID | IndEnz0018000693 |
| Enzyme Type ID | peroxidase000693 |
| Protein Name |
Chorion peroxidase EC 1.11.1.7 |
| Gene Name | pxt AGAP004038 |
| Organism | Anopheles gambiae (African malaria mosquito) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Nematocera Culicomorpha Culicoidea Culicidae (mosquitos) Anophelinae Anopheles Cellia Pyretophorus gambiae species complex Anopheles gambiae (African malaria mosquito) |
| Enzyme Sequence | MLPKGVLLFLVLIVLVQHFATVQTTNAIERPSAPSSQCTSSHESCVLRVMCEVEPRARTTLVPCLTADGLEGVCCSVAKEGKQRKKRSLPFELSQELFQNAVGEGHRVYTRKLANIDHHREVMRGGSVDTLVRQFHAPPGEPLGAEDPTAYEDMFVARSFANALNLSVAERLDLPELTLDPALRRKRCLPPRSCDPHARYRSLDGSCNNPVPARSSWGAAGYPFERLLPPAYEDGVWAPRVHSSVSGRLLASARDISVAVFPDVDRRDRKFNLLLMQFGQFMSHDFTRSASVRIGQEEVQCCNAEHSGALRGEQAHFACMPIAVSPADPFYSRFGIRCLNFVRLALARDGKCRLGYGKQLNRVTHFIDGSAVYGSNEALAASLRTFEGGRLRSSFPTGEELLPFARTRAACEPWAKACFRAGDDRVNQIVSLTEMHTLFLREHNRVATALAALNRHWDDERLYQETRRIVGAVMQKIFYNEYLPSIVGHSKARQYGLLDSHGEQTDFYSPDVKPAVFNELSGAAFRFGHSTVDGAFLIQHRHRRTELVPIQEVFLNPSRLLQRSFFDDFLFSLMDQPQQQLDDSITFGLTRLLFAGRNPFGSDLASLNIQRGRDHALRPYNDYRSWAGLERLTSFEQFGPVGARLASVYEFPDDVDLWVGGLLEPPTQDGALFGETFAAIISEQFARLKFGDRYYYTNGPRTNPGFFTGEQLRELSKVSLASVICANLDQADGFSAPRDAFRQPSEHNPPVPCQTLVGMDLSAWRGH |
| Enzyme Length | 767 |
| Uniprot Accession Number | Q7QH73 |
| Absorption | |
| Active Site | ACT_SITE 284; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P05164, 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 formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Glycosylation (5); Metal binding (1); Modified residue (2); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Acetylation;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Hydroxylation;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Note=In the chorion layer of the mature eggs. {ECO:0000250}. |
| Modified Residue | MOD_RES 188; /note="N-acetylcysteine; in Chorion peroxidase light chain"; /evidence="ECO:0000250"; MOD_RES 331; /note="3',4'-dihydroxyphenylalanine"; /evidence="ECO:0000250|UniProtKB:P82600" |
| Post Translational Modification | PTM: N-glycosylated on Trp by mannose. {ECO:0000250|UniProtKB:P82600}. |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 85,796 |
| Kinetics | |
| Metal Binding | METAL 529; /note="Iron (heme b axial ligand)"; /evidence="ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298" |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |