| IED ID | IndEnz0018000775 |
| Enzyme Type ID | peroxidase000775 |
| Protein Name |
Heme peroxidase 2 EC 1.11.1.7 Cleaved into: Heme peroxidase 2 light chain; Heme peroxidase 2 heavy chain |
| Gene Name | hpx-2 F09F3.5 |
| 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 | MNLKPTILLFTILFLKCATFEVNEETERIVEDAVMRALDSRASENSESEQTSQHIIVSQQANSDSKSAQFTGEVLEEATRILVREFGLEILPAANEVIERWRNEEEELLQSSETTTTTEHPDPTRSKRSAIFRSKRQANRRCSSPPINCNNRFHTSIRSITGLCNNRQNSDLGNSVSPLRRILGAASYADGLGRIRTRSVNGGELPSARLISNRIHDDRNNQVFSPSINHLHMIIGQFIAHDVVFMPSSVARDGGALDCSACNSPQRVSPNCAPITIPRNDPYFNTPCMRLTRALNGQENFGVRSQIGQNSHFLDLSPVYGSADCEAETVRSFQEGKMLTFDDLGYTLPPQNANDSNCQSSAPFHCFTCGDFRNSLHPALIPVHTILIKEHNRLAEQVRVARPRFNDEQIFQLVRKIMIGMWQHIVYNEYIPKYLPRRTIRNFALRPLRNGVHRGYSTSVDPSISAEFAGAAFRFGHSQSRFDFPRLTENGRPAGNYDLGNDIFYADQMYLTRIGGWEPVMNGMVRMPAMKSDRYFSFGIRNQMFEIRGRNGSGVDLVSINIQRGRDMGLFPYIQYRQLVGLPTVTSFNELNTTFSQENIQALRNVYSDPADIDLYVGIMLEEPLSGGQLGPTASFMIGEQFRALKRGDRFFYESIAEGTDNFTQEEISELRNKTSLAKIICTNMDFAARINTDIFDHRSRQVACTSLPQLDIDRFLR |
| Enzyme Length | 718 |
| Uniprot Accession Number | P90820 |
| Absorption | |
| Active Site | ACT_SITE 241; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; Evidence={ECO:0000250|UniProtKB:Q23490}; |
| DNA Binding | |
| EC Number | 1.11.1.7 |
| Enzyme Function | FUNCTION: Peroxidase which is involved in maintaining the cuticle integrity in the hypodermis and pharynx (PubMed:30695063). It thus plays a role in conferring resistance against Gram-positive bacteria such as E.faecalis, S.aureus and C.diphtheriae, and yeast such as C.albicans (PubMed:24621828, PubMed:30695063). {ECO:0000269|PubMed:24621828, ECO:0000269|PubMed:30695063}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Compositional bias (1); Disulfide bond (4); Glycosylation (5); Metal binding (6); Mutagenesis (3); Propeptide (1); Region (2); Signal peptide (1); Site (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Heme;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 11231151; 21367940; 22267497; 22560298; 23800452; 24884423; 25487147; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 81,183 |
| Kinetics | |
| Metal Binding | METAL 242; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 311; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 313; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 315; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 317; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 477; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |