IED ID | IndEnz0002010075 |
Enzyme Type ID | protease010075 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase UCHL3 EC 3.4.19.12 PfUCHL3 |
Gene Name | UCHL3 PF3D7_1460400 |
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 | MAKNDIWTPLESNPDSLYLYSCKLGQSKLKFVDIYGFNNDLLDMIPQPVQAVIFLYPVNDNIVSENNTNDKHNLKENFDNVWFIKQYIPNSCGTIALLHLYGNLRNKFELDKDSVLDDFFNKVNEMSAEKRGQELKNNKSIENLHHEFCGQVENRDDILDVDTHFIVFVQIEGKIIELDGRKDHPTVHCFTNGDNFLYDTGKIIQDKFIEKCKDDLRFSALAVIPNDNFDII |
Enzyme Length | 232 |
Uniprot Accession Number | Q8IKM8 |
Absorption | |
Active Site | ACT_SITE 92; /note=Nucleophile; /evidence=ECO:0000269|PubMed:20042598; ACT_SITE 164; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P09936 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:17371404, ECO:0000269|PubMed:19047059, ECO:0000269|PubMed:20042598, ECO:0000269|PubMed:31658303}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8 (PubMed:17371404, PubMed:31658303, PubMed:20042598). Essential for parasite blood stage survival (PubMed:20042598). {ECO:0000269|PubMed:17371404, ECO:0000269|PubMed:20042598, ECO:0000269|PubMed:31658303}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (7); Chain (1); Helix (9); Mutagenesis (3); Region (3); Site (4); Turn (3) |
Keywords | 3D-structure;Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 2WDT; 2WE6; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 26,899 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=301 nM for ubiquitin-AMC {ECO:0000269|PubMed:20042598}; Note=kcat is 3.2 sec(-1) with ubiquitin-AMC as substrate. {ECO:0000269|PubMed:20042598}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |