| IED ID | IndEnz0002005014 |
| Enzyme Type ID | protease005014 |
| Protein Name |
Desampylase EC 3.4.19.15 JAMM/MPN + metalloprotease PfJAMM1 |
| Gene Name | PF1070 |
| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus furiosus Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Enzyme Sequence | MPSSSKSDFSFSTLIIPQHYLRAILKVVSSSSVEVCGFLFGKENRVLKVRFIRNRLNSPVEFEMDPEEMLKALEEAEQENLEVVGIFHSHIACPPIPSGKDLEGMKRWPVIWLIVNEKGEYKAWILSEKNKISEVKIVVE |
| Enzyme Length | 140 |
| Uniprot Accession Number | Q8U1Y4 |
| Absorption | |
| Active Site | ACT_SITE 34; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:D4GTS4 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA in vitro. {ECO:0000269|PubMed:28479062}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=An N(6)-[small archaeal modifier protein]-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + a [small archaeal modifier protein].; EC=3.4.19.15; Evidence={ECO:0000269|PubMed:28479062}; |
| DNA Binding | |
| EC Number | 3.4.19.15 |
| Enzyme Function | FUNCTION: Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. In vitro, is also able to cleave non-physiological ubiquitin (Ub) substrates, such as 'Met1-', 'Lys48-', and 'Lys63'-linked Ub dimers (Ub2), and to remove Ub tags from diverse proteins. {ECO:0000269|PubMed:28479062}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 100 degrees Celsius. {ECO:0000269|PubMed:28479062}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Disulfide bond (1); Domain (1); Helix (3); Metal binding (3); Motif (1); Mutagenesis (6); Site (1) |
| Keywords | 3D-structure;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The disulfide bridge probably stabilizes the PfJAMM1 homodimer at the optimal growth temperature of the hyperthermophile. {ECO:0000305|PubMed:28479062}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5LD9; 5LDA; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 88..101; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 16,018 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.2 uM for SAMP2 dimer (with PfJAMM1 in the dimeric form, at 100 degrees Celsius) {ECO:0000269|PubMed:28479062}; KM=15.5 uM for SAMP2 dimer (with PfJAMM1 in the monomeric form, at 100 degrees Celsius) {ECO:0000269|PubMed:28479062}; KM=155 uM for M1-linked Ub dimer (with PfJAMM1 in the monomeric form, at 70 degrees Celsius) {ECO:0000269|PubMed:28479062}; Note=kcat is 0.28 min(-1) for the cleavage of SAMP2 dimer using PfJAMM1 in the dimeric form. kcat is 0.16 min(-1) for the cleavage of SAMP2 dimer using PfJAMM1 in the monomeric form (at 100 degrees Celsius). kcat is 0.0016 min(-1) for the cleavage of M1-linked Ub dimer using PfJAMM1 in the monomeric form (at 70 degrees Celsius). {ECO:0000269|PubMed:28479062}; |
| Metal Binding | METAL 88; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000269|PubMed:28479062, ECO:0007744|PDB:5LD9"; METAL 90; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000269|PubMed:28479062, ECO:0007744|PDB:5LD9"; METAL 101; /note="Zinc"; /evidence="ECO:0000269|PubMed:28479062, ECO:0007744|PDB:5LD9" |
| Rhea ID | |
| Cross Reference Brenda |