| IED ID | IndEnz0002005939 |
| Enzyme Type ID | protease005939 |
| Protein Name |
Falcilysin EC 3.4.24.- |
| Gene Name | FLN PFHG_03273 |
| 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 | MNLTKLMKVFGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQYLGQLDYSKYRDDAVESVEYQTYKKGPFYIKKKYGDHSEEKENLVSVAWLLNPKVDKTNNHNNNHSNNQSSENNGYSNGSHSSDLSLENPTDYFVLLIINNLLIHTPESVLYKALTDCGLGNNVIDRGLNDSLVQYIFSIGLKGIKRNNEKIKIFDKVHYEVEDVIMNALKKVVKEGFNKSAVEASINNIEFILKEANLKTSKSIDFVFEMTSKLNYNRDPLLIFEFEKYLNIVKNKIKNEPMYLEKFVEKHFINNAHRSVILLEGDENYAQEQENLEKQELKKRIENFNEQEKEQVIKNFEELSKYKNAEESPEHLNKFPIISISDLNKKTLEVPVNVYFTNINENNNIMETYNKLKTNEHMLKDNMDVFLKKYVLKNDKHNTNNNNNNNNNMDYSFTETKYEGNVPILVYEMPTTGIVYLQFVFSLDHLTVDELAYLNLFKTLILENKTNKRSSEDFVILREKNIGSMSANVALYSKDDHLNVTDKYNAQALFNLEMHVLSHKCNDALNIALEAVKESDFSNKKKVIDILKRKINGMKTTFSEKGYAILMKYVKAHLNSKHYAHNIIYGYENYLKLQEQLELAENDFKTLENILVRIRNKIFNKKNLMVSVTSDYGALKHLFVNSNESLKNLVSYFEENDKYINDMQNKVNDPTVMGWNEEIKSKKLFDEEKVKKEFFVLPTFVNSVSMSGILFKPGEYLDPSFTVIVAALKNSYLWDTVRGLNGAYGVFADIEYDGSVVFLSARDPNLEKTLATFRESAKGLRKMADTMTENDLLRYIINTIGTIDKPRRGIELSKLSFLRLISNESEQDRVEFRKRIMNTKKEDFYKFADLLESKVNEFEKNIVIITTKEKANEYIANVDGEFKKVLIE |
| Enzyme Length | 1193 |
| Uniprot Accession Number | A0A0L7KF24 |
| Absorption | |
| Active Site | ACT_SITE 132; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:10542284, PubMed:12876284). In the apicoplast, degrades apicoplast transit peptides after their cleavage (By similarity). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (PubMed:12876284). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (PubMed:12876284). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (PubMed:12876284). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (PubMed:12876284). {ECO:0000250|UniProtKB:Q76NL8, ECO:0000269|PubMed:10542284, ECO:0000269|PubMed:12876284}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 (food vacuole) (PubMed:12876284). Optimum pH is 7 (PubMed:12876284). {ECO:0000269|PubMed:12876284}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Coiled coil (1); Metal binding (3) |
| Keywords | Apicoplast;Coiled coil;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Metalloprotease;Plastid;Protease;Reference proteome;Vacuole;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10542284}; Peripheral membrane protein {ECO:0000269|PubMed:12876284}. Plastid, apicoplast {ECO:0000250|UniProtKB:Q76NL8}. Vesicle {ECO:0000269|PubMed:12876284}. Note=Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:10542284, PubMed:12876284). During the trophozoite and early to mid-schizont stages, localizes to the apicoplast (By similarity). {ECO:0000250|UniProtKB:Q76NL8, ECO:0000269|PubMed:10542284, ECO:0000269|PubMed:12876284}. |
| Modified Residue | |
| Post Translational Modification | PTM: Does not require processing for targeting to the food vacuole or maturation. {ECO:0000269|PubMed:12798513, ECO:0000269|PubMed:12876284}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 138,896 |
| Kinetics | |
| Metal Binding | METAL 129; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q76NL8; METAL 133; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q76NL8; METAL 243; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q76NL8 |
| Rhea ID | |
| Cross Reference Brenda |