| IED ID | IndEnz0018001494 |
| Enzyme Type ID | peroxidase001494 |
| Protein Name |
Peroxidasin EC 1.11.2.- |
| Gene Name | Pxn CG12002 |
| Organism | Drosophila melanogaster (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 melanogaster (Fruit fly) |
| Enzyme Sequence | MRFMLLMLQLLGLLLLLAGGVQSVYCPAGCTCLERTVRCIRAKLSAVPKLPQDTQTLDLRFNHIEELPANAFSGLAQLTTLFLNDNELAYLQDGALNGLTALRFVYLNNNRLSRLPATIFQRMPRLEAIFLENNDIWQLPAGLFDNLPRLNRLIMYNNKLTQLPVDGFNRLNNLKRLRLDGNAIDCNCGVYSLWRRWHLDVQRQLVSISLTCAAPQMLQNQGFSSLGEHHFKCAKPQFLVAPQDAQVAAGEQVELSCEVTGLPRPQITWMHNTQELGLEEQAQAEILPSGSLLIRSADTSDMGIYQCIARNEMGALRSQPVRLVVNGGNHPLDSPIDARSNQVWADAGTPMHGATPLPSPLPSPPHFTHQPHDQIVALHGSGHVLLDCAASGWPQPDIQWFVNGRQLLQSTPSLQLQANGSLILLQPNQLSAGTYRCEARNSLGSVQATARIELKELPEILTAPQSQTIKLGKAFVLECDADGNPLPTIDWQLNGVPLPGNTPDLQLENENTELVVGAARQEHAGVYRCTAHNENGETSVEATIKVERSQSPPQLAIEPSNLVAITGTTIELPCQADQPEDGLQISWRHDGRLIDPNVQLAEKYQISGAGSLFVKNVTIPDGGRYECQLKNQFGRASASALVTIRNNVDLAPGDRYVRIAFAEAAKEIDLAINNTLDMLFSNRSDKAPPNYGELLRVFRFPTGEARQLARAAEIYERTLVNIRKHVQEGDNLTMKSEEYEFRDLLSREHLHLVAELSGCMEHREMPNCTDMCFHSRYRSIDGTCNNLQHPTWGASLTAFRRLAPPIYENGFSMPVGWTKGMLYSGHAKPSARLVSTSLVATKEITPDARITHMVMQWGQFLDHDLDHAIPSVSSESWDGIDCKKSCEMAPPCYPIEVPPNDPRVRNRRCIDVVRSSAICGSGMTSLFFDSVQHREQINQLTSYIDASQVYGYSTAFAQELRNLTSQEGLLRVGVHFPRQKDMLPFAAPQDGMDCRRNLDENTMSCFVSGDIRVNEQVGLLAMHTIWMREHNRIASKLKQINSHWDGDTLYQEARKIVGAQMQHITFKQWLPLIIGESGMEMMGEYQGYNPQLNPSIANEFATAALRFGHTIINPILHRLNETFQPIPQGHLLLHKAFFAPWRLAYEGGVDPLMRGFLAVPAKLKTPDQNLNTELTEKLFQTAHAVALDLAAINIQRGRDHGMPGYNVYRKLCNLTVAQDFEDLAGEISSAEIRQKMKELYGHPDNVDVWLGGILEDQVEGGKVGPLFQCLLVEQFRRLRDGDRLYYENPGVFSPEQLTQIKQANFGRVLCDVGDNFDQVTENVFILAKHQGGYKKCEDIIGINLYLWQECGRCNSPPAIFDSYIPQTYTKRSNRQKRDLGKENDEVATAESYDSPLESLYDVNEERVSGLEELIGSFQKELKKLHKKLRKLEDSCNSADSEPVAQVVQLAAAPPQLVSKPKRSHCVDDKGTTRLNNEVWSPDVCTKCNCFHGQVNCLRERCGEVSCPPGVDPLTPPEACCPHCPMVK |
| Enzyme Length | 1527 |
| Uniprot Accession Number | Q9VZZ4 |
| Absorption | |
| Active Site | ACT_SITE 863; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 862; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"; BINDING 1015; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + H2O2 + L-methionyl-[collagen] = [collagen]-(5R)-5-hydroxy-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66008, Rhea:RHEA-COMP:12752, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16950, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:133442, ChEBI:CHEBI:166866; Evidence={ECO:0000269|PubMed:22842973};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66009; Evidence={ECO:0000269|PubMed:22842973}; CATALYTIC ACTIVITY: Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:29250; Evidence={ECO:0000269|PubMed:22842973};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017; Evidence={ECO:0000269|PubMed:22842973}; CATALYTIC ACTIVITY: Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + hypobromite + L-methionyl-[collagen] = [collagen]-(5R)-5-hydroxy-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O; Xref=Rhea:RHEA:66012, Rhea:RHEA-COMP:12752, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16950, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250, ChEBI:CHEBI:133442, ChEBI:CHEBI:166866; Evidence={ECO:0000269|PubMed:22842973};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66013; Evidence={ECO:0000269|PubMed:22842973}; CATALYTIC ACTIVITY: Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969, ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O; Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250, ChEBI:CHEBI:29969, ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512; Evidence={ECO:0000250|UniProtKB:Q92626};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512; Evidence={ECO:0000250|UniProtKB:Q92626};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357; Evidence={ECO:0000250|UniProtKB:Q92626}; |
| DNA Binding | |
| EC Number | 1.11.2.- |
| Enzyme Function | FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV NC1 hexamer (PubMed:22842973). Plays a role in extracellular matrix consolidation, phagocytosis and defense (PubMed:8062820). {ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:8062820}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Binding site (2); Chain (1); Coiled coil (1); Disulfide bond (12); Domain (6); Frameshift (1); Glycosylation (9); Metal binding (6); Repeat (6); Sequence conflict (11); Signal peptide (1); Site (1) |
| Keywords | Alternative splicing;Calcium;Coiled coil;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Immunoglobulin domain;Iron;Leucine-rich repeat;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10373118; 11139274; 11677054; 11955438; 12091301; 12167411; 12374748; 12426388; 12459925; 12586708; 12810602; 14602069; 14605208; 14623821; 14657024; 15020472; 15179511; 15239955; 15561773; 15699212; 15708571; 15857916; 15907832; 16176949; 16277749; 16369566; 16618604; 16651377; 17705839; 18418383; 18632567; 19598118; 19799768; 19934223; 20023157; 20220848; 20371351; 20483458; 20688956; 20708591; 21074052; 21124962; 21264297; 21509534; 21688401; 22275438; 22411814; 22724070; 22743648; 22951642; 22952763; 22976306; 22976969; 23071443; 23840627; 24029952; 24412417; 24613936; 24675402; 24707047; 24778181; 24906154; 24946019; 25201876; 25242144; 25294943; 25294944; 25417159; 25628309; 25687947; 25739458; 25740935; 25824290; 25943032; 25995252; 26121667; 26162375; 26202798; 26289344; 26353752; 26551273; 26568309; 26587980; 26859824; 26870755; 27058248; 27794539; 28237966; 28280122; 28369070; 28993397; 29191551; 29565247; 29656148; 29670218; 30022065; 30292413; 30733377; 30837285; 30923041; 31093969; 31138608; 31453329; 31722958; 31992650; 32082322; 32487456; 32598400; 32722007; 32727922; 32900993; 33131706; 33274675; 33322177; 33594977; 33717711; 33748138; 33767161; 34713801; 34722521; 7760738; 9356176; 9362473; 9540809; 9630744; |
| Motif | |
| Gene Encoded By | |
| Mass | 170,514 |
| Kinetics | |
| Metal Binding | METAL 864; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 941; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 943; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 945; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 947; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 1109; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:66008; RHEA:66009; RHEA:66016; RHEA:66017; RHEA:66012; RHEA:66013; RHEA:66020; RHEA:66021; RHEA:66024; RHEA:66025; RHEA:69360; RHEA:69361; RHEA:69356; RHEA:69357 |
| Cross Reference Brenda |