Detail Information for IndEnz0002008305
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