| IED ID | IndEnz0018001543 |
| Enzyme Type ID | peroxidase001543 |
| Protein Name |
Peroxidasin EC 1.11.2.- Cleaved into: PXDN active fragment |
| Gene Name | pxdn pxn |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MAGAGSWLYLTAGLLVVALPQLSHSCPSRCLCFRTTVRCMHLMLESVPAVPPHTTILDLRFNRIKDIQTGAFKHLKNLNTLLLNNNQIKRIPSEAFKDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLEPESFNYLPKLERLFLHNNRITHLVPGTFSQLESMKRLRLDSNALHCDCEILWLADLLKIYSESGNAQAAATCEYPRRLQGRSVSTITPSELNCERPRITSEPQDVDVTFGNTVYFTCRAEGNPKPEIIWLRNNNELSMKDDSRLNLLNDGTLMIQNTKETDQGIYQCMAKNVAGEVKTHEVTLRYYGTPATPTFVIQPQNTEVLVGESVTLECSATGQPHPRVTWTRGDRTPLPSDPRINITPSGGLYIQNVNQDDAGEYTCFATNSVETIHSTAYIIVQAVPQFTVVPQDRNVFEGHTVDFHCEAQGNPKPVIAWTKGGNQLSVDRRHQVLSSGTLRILRVALHDQGQYECQAVNIVGSKSTAAQLIVQTRVTPVFATVPNDMTVEVGTDVQIPCSSQGDPLPIITWNKDGIQVTESGKFHISPHGYLAIRDAGLADQGRYECVARNPIGYSSVSMVLSVLVPEVSRTGDPFVATSIIEAIATVDRAINSTRTHLFDSRPRSPGDLLALFRYPRDPYTVEQARAAEIFERTLQLIQDHVQSGLMVDLNGTSYHYNDLVSPQYLNMIANLSGCATHRRINNCSNMCFHQKYRTHDGTCNNLQHPMWGASLTAFERLLKSVYENGFNLPRGISGRIYNGFPLPLPRLVSTTLIGTHTITPDEQFTHMLMQWGQFLDHDLDSTVVALSQARFSDGQDCSVVCTNDAPCFPIMVPPNDPRVRNNARCMSMVRSSPVCGSGMTSLLMNSVYPREQMNQLTSYIDASNVYGSSDHESNEIRDSASHRGLLKQGIVQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIATELLRLNPHWDGDTIYHETRKIVGAQMQHITYSHWLPKIFGDVGMKMLGEYKSYDPNVNAGILNEFATAAFRFGHTLINPILYRLDEKFEPIPQGHVPLHRAFFSPFRIVNEGGIDPLLRGLIGVAAKMRVTSQLLNTELTEKLFSMAHAVALDLAALNVQRGRDHGIPPYHDFRVFCNLSTVQTFDDLRNEIKNPDVREKLKRLYGSPLNIDLFPALMVEDLIPGSRLGPTLMCLLTTQFRNIRDGDRFWYENPGVFTAAQLTQIKQTSLARVLCDNGDNITKVQHDLFRVAEFPHGYVSCKNIAKMDLRVWQDCCEDCRTRGQFSTFSNHFRGKRSTEHSYKEDNKEPSSLLNQSVNTTCNTEQPKNLPHVNDFKEFVLDMQKTITGLRKQIKKLESRLSNTDCTDETGESHSTKEKWNKDACTKCECYNGHITCFVKSCPPVNCSRPQRIEGVCCPVCTDDKIQST |
| Enzyme Length | 1457 |
| Uniprot Accession Number | A4IGL7 |
| Absorption | |
| Active Site | ACT_SITE 816; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 815; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"; BINDING 969; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" |
| Calcium Binding | |
| catalytic Activity | 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=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:29250; Evidence={ECO:0000250|UniProtKB:Q92626};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017; 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/COL4A1 NC1 hexamer and participates to the basement membrane integrity. Moreover brominates alpha2 collagen IV chain/COL4A2 and leads to bromine enrichment of the basement membranes. {ECO:0000250|UniProtKB:Q92626}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (2); Disulfide bond (17); Domain (7); Erroneous initiation (1); Glycosylation (9); Metal binding (6); Region (1); Repeat (6); Signal peptide (1); Site (2) |
| Keywords | Basement membrane;Calcium;Disulfide bond;Endoplasmic reticulum;Extracellular matrix;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, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q92626}. Cell surface {ECO:0000250|UniProtKB:Q92626}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q3UQ28}. Note=Enriched in the peritubular space of fibrotic kidneys. Adheres on the cell surface in 'hot spots'. {ECO:0000250|UniProtKB:Q92626}.; SUBCELLULAR LOCATION: [PXDN active fragment]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92626}.; PTM: Processed by FURIN and the proteolytic processing largely depends on the peroxidase activity of PXDN (By similarity). The proteolytic cleavage occurs after intracellular homotrimerization and releases into the extracellular matrix a large, catalytically active fragment and a smaller fragment consisting primarily of the C-terminal VWFC domain. The processing enhances both peroxidase activity and sulfilimine cross-links formation (By similarity). {ECO:0000250|UniProtKB:Q92626}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 163,914 |
| Kinetics | |
| Metal Binding | METAL 817; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 896; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 898; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 900; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 902; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 1063; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:66020; RHEA:66021; RHEA:66016; RHEA:66017; RHEA:66024; RHEA:66025; RHEA:69360; RHEA:69361; RHEA:69356; RHEA:69357 |
| Cross Reference Brenda |