| IED ID | IndEnz0018001693 |
| Enzyme Type ID | peroxidase001693 |
| Protein Name |
Peroxidasin homolog pxn-2 EC 1.11.2.- |
| Gene Name | pxn-2 K09C8.5 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MLLEFLLLIGISLSTACPSECRCAGLDVHCEGKNLTAIPGHIPIATTNLYFSNNLLNSLSKSNFQALPNLQYLDLSNNSIRDIEETLLDSFPGLKYLDLSWNKIRYVPKLSTAPNALVSLNLVHNEISRLDNDLVSHSPYMQTFLIQRNRIQSLPHDFFNSRMVPTLKTVKMAGNPWSCDCRMVNVKQFADSLFAHSNQNIFIVGKCFFPKGLRNYVFRNLSIENLECEKPEYSKTDDGMFKMSCPNNEMEGYHYDSIFLENNKEARHTAHFARDKDGSLLSNGQFTRNYQCAFYRQKQSIHMQKKMQASSSTEPPITTTTMEPMTTSTMDSMDTTESVVTMTTMPEIDTKIVFEHKQLDTTSRDGETLELKCEASGEPTPTITWLFEKQKLTESRKHKLTKNGSVLKIFPFLNTDIGQYECVASNGEESKSHIFSVSLKESEQPVIIDAPMDTNATIGQQVTLRCNAKGFPVPDVVWLFEGIRIPRRNTRYTISDNNIELTIEKVTRHDSGVFTCQAVNSVGSAVATANLLVGAELTEKVDKLLDDSTIEKIAKEAKQKVEKALSSTKDQQRMDKIESPNDLSKLFKFAINLKKVDLGKAREIYEESIRLVQMHIDNGLAFESAMISPNVSYEAVLPVSYVQTLMEKSGCQTGQFAESCEDHCFFSKYRSYDGQCNNHEHPWWGVSEMAFMRLLPPRYENGFNTPVGWEKGKRYNGYEVPNARKVSRVLIGTDETTPHSHLSAMTMQWGQFIDHDLTLTAPALTRHSYKEGAFCNRTCENADPCFNIQLEADDPKLHTGLYQKHPCMEFERNGAACGSGETSPIFQRVTYRDQLNLLTSYLDASGIYGNSEEQALELRDLYSDHGLLRFDIVSGANKPYMPFEKDSDMDCRRNFSRENPIKCFLAGDVRANEQLGLMSMHTIFLREHNRIASRLLEVNENWDGETIFQETRKLIGAMLQHITYNAWLPKILGKATYNTIIGEYKGYNPDVNPTIANEFATAALRFAHTLINTHLFRFDKDFKETKQGHLPLHNAFFAPERLVSEGGVDPLLRGLFAAPIKMPRPDQVLNKELTEKLFNRFHEVALDLAALNIQRGRDHGLPSWTEYRKFCNLTVPKTWSDMKNIVQNDTVISKLQSLYGVTENIDLWVGGVTEKRTADALMGPTLACIIADQFKRLRDGDRFWYENEEMFSKAQLRQIKKVTLSKIICTNGDDIDRIQRDIFVYHGNSTQFYEPCESLPEINLNMWTTCCDAMCSSSSTLARNAIGGDEKAKRRKRRHHHSKKSCHDKGKRRKSGDRWNHSNDICVECMCHDGEVWCKTNNFCKSQV |
| Enzyme Length | 1328 |
| Uniprot Accession Number | G5EG78 |
| Absorption | |
| Active Site | ACT_SITE 755; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | BINDING 754; /note=Heme b; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; BINDING 913; /note=Heme b; covalent; /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 (By similarity). Required for embryonic morphogenesis playing a role in epidermal elongation at the twofold stage of embryonic development (PubMed:20876652). Required post-embryonically for basement membrane integrity and muscle-epidermal attachments, and specifically in the function of basement membrane components such as the type IV collagens (PubMed:20876652, PubMed:29440357). May have a role in inhibiting axon regeneration (PubMed:20876652). May functionally antagonize the peroxidasin pxn-1 (PubMed:20876652). {ECO:0000250|UniProtKB:Q92626, ECO:0000269|PubMed:20876652, ECO:0000269|PubMed:29440357}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Glycosylation (12); Metal binding (6); Mutagenesis (5); Region (2); Repeat (8); Signal peptide (1); Site (1) |
| Keywords | Basement membrane;Disulfide bond;Extracellular matrix;Glycoprotein;Heme;Iron;Leucine-rich repeat;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20876652, ECO:0000269|PubMed:25475546}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:20876652}. Note=Localizes to the basement membrane in between the epidermis and muscles. {ECO:0000269|PubMed:20876652}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 16049479; 20439776; 21177967; 22267497; 22286215; 22560298; 23800452; 24884423; 25487147; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 151,152 |
| Kinetics | |
| Metal Binding | METAL 756; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 839; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 841; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 843; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 845; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 1008; /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 |