IED ID | IndEnz0002008305 |
Enzyme Type ID | protease008305 |
Protein Name |
Plasmepsin X PfPMX EC 3.4.23.- Plasmepsin 10 |
Gene Name | PMX PF3D7_0808200 |
Organism | Plasmodium falciparum (isolate 3D7) |
Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
Enzyme Sequence | MKRISPLNTLFYLSLFFSYTFKGLKCTRIYKIGTKALPCSECHDVFDCTGCLFEEKESSHVIPLKLNKKNPNDHKKLQKHHESLKLGDVKYYVNRGEGISGSLGTSSGNTLDDMDLINEEINKKRTNAQLDEKNFLDFTTYNKNKAQDISDHLSDIQKHVYEQDAQKGNKNFTNNENNSDNENNSDNENNSDNENNLDNENNLDNENNSDNSSIEKNFIALENKNATVEQTKENIFLVPLKHLRDSQFVGELLVGTPPQTVYPIFDTGSTNVWVVTTACEEESCKKVRRYDPNKSKTFRRSFIEKNLHIVFGSGSISGSVGTDTFMLGKHLVRNQTFGLVESESNNNKNGGDNIFDYISFEGIVGLGFPGMLSAGNIPFFDNLLKQNPNVDPQFSFYISPYDGKSTLIIGGISKSFYEGDIYMLPVLKESYWEVKLDELYIGKERICCDEESYVIFDTGTSYNTMPSSQMKTFLNLIHSTACTEQNYKDILKSYPIIKYVFGELIIELHPEEYMILNDDVCMPAYMQIDVPSERNHAYLLGSLSFMRNFFTVFVRGTESRPSMVGVARAKSKN |
Enzyme Length | 573 |
Uniprot Accession Number | Q8IAS0 |
Absorption | |
Active Site | ACT_SITE 266; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 457; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by small molecule 49c (PubMed:29074775). Inhibited by small molecules WM382, WM4, and WM5 (PubMed:32109369). {ECO:0000269|PubMed:29074775, ECO:0000269|PubMed:32109369}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: During the asexual blood stage, processes key proteins essential for merozoite egress and invasion of host erythrocytes (PubMed:29074775, PubMed:32109369). Cleaves and activates proteases SUB1 and SUB2 (PubMed:29074775, PubMed:32109369). May process members of the EBL and Rh protein families (PubMed:32109369). Also cleaves apical membrane protein AMA1 (PubMed:29074775). During the mosquito vector stage and probably in ookinetes, cleaves CelTOS (PubMed:29074775). {ECO:0000269|PubMed:29074775, ECO:0000269|PubMed:32109369}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (1); Mutagenesis (1); Propeptide (1); Region (1); Signal peptide (1) |
Keywords | 3D-structure;Aspartyl protease;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:W7JWW5}. Note=In schizonts, localizes to exonemes which are secretory vesicles that discharge their content during egress into the parasitophorous vacuole. {ECO:0000250|UniProtKB:W7JWW5}. |
Modified Residue | |
Post Translational Modification | PTM: Autocleaved into a p16 prodomain form and two mature forms p44 and p51. {ECO:0000269|PubMed:32109369}. |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 6ORS; |
Mapped Pubmed ID | 16267556; |
Motif | |
Gene Encoded By | |
Mass | 65,114 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |