| IED ID | IndEnz0002001468 |
| Enzyme Type ID | protease001468 |
| Protein Name |
Plasmepsin III EC 3.4.23.39 Histo-aspartic protease Plasmepsin 3 |
| Gene Name | PMIII HAP PFHG_00466 |
| Organism | Plasmodium falciparum (isolate HB3) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate HB3) |
| Enzyme Sequence | MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL |
| Enzyme Length | 451 |
| Uniprot Accession Number | Q9Y006 |
| Absorption | |
| Active Site | ACT_SITE 337; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | ACTIVITY REGULATION: Dimerization causes loss of catalytic activity (By similarity). Inhibited by pepstatin A (PubMed:11782538). {ECO:0000250|UniProtKB:Q8IM15, ECO:0000269|PubMed:11782538}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO(2))-Ser-Phe-Pro-Thr.; EC=3.4.23.39; Evidence={ECO:0000269|PubMed:11782538}; |
| DNA Binding | |
| EC Number | 3.4.23.39 |
| Enzyme Function | FUNCTION: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins (PubMed:11782538). Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). {ECO:0000269|PubMed:11782538, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.7. {ECO:0000269|PubMed:11782538}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Propeptide (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Aspartyl protease;Disulfide bond;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Vacuole lumen {ECO:0000269|PubMed:11782538}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:11782538}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved into the soluble active mature form by cysteine proteases in the digestive vacuole of trophozoites (PubMed:12850260). Proteolysis requires an acidic environment (By similarity). Transprocessing may serve as an alternate activation system (Probable). {ECO:0000250|UniProtKB:P39898, ECO:0000269|PubMed:12850260, ECO:0000305|PubMed:32385863}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3QVC; 3QVI; 6KUB; 6KUC; 6KUD; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |