IED ID | IndEnz0018000009 |
Enzyme Type ID | peroxidase000009 |
Protein Name |
Peroxidase mlt-7 EC 1.11.1.7 Molting defective protein 7 MoLT-7 Cleaved into: Peroxidase mlt-7 light chain; Peroxidase mlt-7 heavy chain |
Gene Name | mlt-7 ZK430.8 |
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 | MRRLHRNLSLLFLICILNEYRIESQTLSPPITDRFKCLTNGCCDHHEWCRFWASIGECNANKDWMTENCQLACGTCTAPAAPLLPVTTTASSFNGGGFVQTTTQSSGPTTTITIPPSSLTSVTSCERVKDSIAQASELMSISRLINPVEDNFGRNMLSIDDITRSVPTGCVPQLSDVGVDCRKSLCYHLMYRTLDGTCNNLEKPMQGAAFRRFNRHFPAQYDDGKGEPISSLNQSRPSAREANRVMLSSAQSVVHDKFNNMMMQWGQFMSHDMSKTTLQPSANCKTCDPVPSKCMPIPIGEKDPNLGFKSKQCLKVSRSAPICRVEPREQLNENTAYIDGSMIYGSSLKDLHKFRDGRTGFLRVTRFNNQNVLPFDQSKCANKDKCTASFTAGDIRANLFIGLSSLHIMFAREHNRIAQKLTELNPTWSGDRVFQEARKIVGAQIQNVLYKEYLPKLLGVSFDKVIGPYKGYDTNVDATIANEFTTSAFRFGHGMIEEFYKRVDLSGNNITHGGFFFGDGVFKSGKILFEGGVDPIIRGFMTTAVKRPHRMTPAITEKMFGSTDLGSLNIQRGRDHGIPSYNKMRQFCGLKSANTFDDFADMILDRNLRAGLARNYNTTNDVDFYVGSMLEDPVIGGLVGTTLSCAIGEQFKRARDGDRFYFENPGIFTRSQMEEIKKSSLSRIICDNADNFELVSQDAFLLPGSNLTPCSKIPKMDLSKWRAL |
Enzyme Length | 724 |
Uniprot Accession Number | Q23490 |
Absorption | |
Active Site | ACT_SITE 271; /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:0000269|PubMed:19406744}; |
DNA Binding | |
EC Number | 1.11.1.7 |
Enzyme Function | FUNCTION: Plays an essential role in cuticle biogenesis. Required in combination with bli-3 for correct formation of cross-links in cuticle collagens. {ECO:0000269|PubMed:19406744}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (2); Disulfide bond (4); Domain (1); Glycosylation (4); Metal binding (6); Propeptide (1); Signal peptide (1); Site (1) |
Keywords | Calcium;Developmental protein;Disulfide bond;Glycoprotein;Heme;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10778742; 11231151; 12097347; 12529635; 14551910; 15084750; 15489339; 16122351; 20439774; 20439776; 20610404; 21085631; 21177967; 21367940; 22267497; 22286215; 22560298; 22921415; 23028364; 23800452; 24884423; 25487147; 6593563; |
Motif | |
Gene Encoded By | |
Mass | 80,829 |
Kinetics | |
Metal Binding | METAL 272; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 335; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 337; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 339; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 341; /note=Calcium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 493; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Rhea ID | RHEA:56136 |
Cross Reference Brenda |