Detail Information for IndEnz0018001564
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