IED ID | IndEnz0018001564 |
Enzyme Type ID | peroxidase001564 |
Protein Name |
Peroxidasin homolog EC 1.11.2.- |
Gene Name | pxn-1 CBG01526 |
Organism | Caenorhabditis briggsae |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis briggsae |
Enzyme Sequence | MNLLLYLLLLVPWVLGSEDGCPAKCTCDKKGFTVDCSNAGLTRIPKGISSNVRSLVLRNNRIHTLIKSDLEGFPLLESLVLTHNKIKVVEENILDHLPELKRLSLSHNLLVYIPPLASESRPLASLNLKRNHIQFIDERWLLQYFPELVQIDLSHNRIQSLRTKLFENLPSLTHAHLHANPWNCDCRVTKVKALLRKVEWERKAYCTNPVELRHQAIDEVEESLLKCAKPEEESWTGDEFKLVCTKNASSSRPVVWLYENAEVDSSSLDGYEIHDSVITVPRKTNVNQMTCTYDYEHVPHHRRLRQSHHSNGAPQFTYKPRDNSYREGSEVKVNCEVMGTPKPSITWYHNGVRFASSRKKQLGLSNNVLRIYPFLEEDSGRYTCEAVNSLGKVSHTFSLDLISSIPPNIYEGPQSVSQNIGGEVVFVCKAKGNPTPDYTWSFDGSTIGHIKGRFMVSDDGTELXISNIEKKDEGYYSCMAGNPVGAMSADAKLTVIGGETRKSSTPQIDEELLRAIAQKARQNVESAVEKTRKQLNQDKITNTNDLKRLFRFSTPKQAVELSKAREIYEESVRLVREHVEKGLILNVDELHPNNVSYESVLHVTHVQALMGLSGCHTGQFKNPCTDTCFHNKYRSFDGQCNNKNKPMNGVSLMPLRRLLKPVYENGFNTPVGWEKGKLYNGYPMPNVREVSRQLVATETITPHRKLSSMVMQWGQFVDHDLTHTVTALSRHSYATGAFCNRTCDNLDPCFNIPLSPSDPRVISESAKYPCIEFERSAAVCGSGETSLVFNRVTYREQMNALTSFLDASNVYGSNEVQAQELRDTYNNNGQLRYDITSAAGKEYLPFEKDSNMDCRRNFSEENPIRCFLAGDLRANEQLALAATHTIFVREHNRIAKKLKKMNGNWDGEVIYHETRKIIGAMMQHITFKHWLPVVFGGQEQMDKFVGKYQGYDPAIDSSVTNAFATAAFRFGHTIINPTLFRLGNDFMSIKQGHIALHKAFFTPELVLTEGGIDPLLRGLFASPLKHPMPTQLLNMELIEKLFMKGHEVSLDLAVMNIQRSRDHGLPSYTEYRQFCNLPVPARWEDMKGYIKDDMIIQKLRGLYGVPQNIDLWVGGIVEEKLENGLFGPTFACIIGEQFRKMRDGDRFWYEKDGVFTPEQMKEIKKVTLARLLCDNGDEIDRIQKDVFMYPGKEKENYGRCEDTEMMDLKAWSKCCDDVCPTMLDRILRSRHRGSRLHGCNQNGLWRPEGAKWIPPNEYCTEEAVFGAPPKKTVLTTEVHSSQRNSVLY |
Enzyme Length | 1288 |
Uniprot Accession Number | A8WQH2 |
Absorption | |
Active Site | ACT_SITE 719; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Activity Regulation | |
Binding Site | BINDING 718; /note="Heme b; covalent, via 2 links"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"; BINDING 876; /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 NC1 hexamer (By similarity). Plays a role in the attachment of tissues and in axonal guidance during early developmental stages (By similarity). May functionally antagonize the peroxidasin pxn-2 to maintain neuronal development (By similarity). {ECO:0000250|UniProtKB:Q1ENI8, ECO:0000250|UniProtKB:Q92626}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Binding site (2); Chain (1); Disulfide bond (7); Domain (4); Glycosylation (4); Metal binding (6); Repeat (12); Signal peptide (1); Site (1) |
Keywords | Calcium;Coiled coil;Disulfide bond;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:Q1ENI8}. Note=Localizes to the extracellular space in between body wall muscle cells. {ECO:0000250|UniProtKB:Q1ENI8}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 146,519 |
Kinetics | |
Metal Binding | METAL 720; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 802; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 804; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 806; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 808; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 972; /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 |