| IED ID | IndEnz0002013802 |
| Enzyme Type ID | protease013802 |
| Protein Name |
CAAX prenyl protease 2 EC 3.4.-.- Intramembrane protease Rce1 IMP Rce1 Prenyl protein-specific endoprotease 2 Ras and a-factor-converting enzyme 1 |
| Gene Name | rce1 MMP0485 |
| Organism | Methanococcus maripaludis (strain S2 / LL) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Methanomada group Methanococci Methanococcales Methanococcaceae Methanococcus Methanococcus maripaludis (Methanococcus deltae) Methanococcus maripaludis (strain S2 / LL) |
| Enzyme Sequence | MISSYKYNPKLYFLSTFVVTYILWFTGAYLSFSSTYSGIYMLIMLPGLMAPFIISTILIAKSKNNELKKDFINRLFNLKLINLKTIPVVFLLMPAVILLSILLSIPFGGSISQFQFSGGFSFSTDFVPVLFLLLLAATFEELGWRGYAFDSLQSRYSLFKASILFGIFWSLWHFPLIFVNNSYQYEIFNQSIWYGLNFFLSILPMGIIITWMCLKNRKSIILAIIFHFLINLNQELLAITQDTKIIETGVLFLVAAAIILYDKKMFFEKLG |
| Enzyme Length | 271 |
| Uniprot Accession Number | Q6LZY8 |
| Absorption | |
| Active Site | ACT_SITE 140; /note=Proton donor/acceptor; /evidence=ECO:0000269|PubMed:24291792; ACT_SITE 173; /note=Proton donor/acceptor; /evidence=ECO:0000269|PubMed:24291792 |
| Activity Regulation | ACTIVITY REGULATION: Activity is unaffected by metalloprotease inhibitors 5 mM EDTA and 5 mM Zn(2+). Activity partially inhibited by 1,10-phenanthroline and 1,7-phenanthroline. {ECO:0000269|PubMed:24291792}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Endopeptidase which proteolytically removes the C-terminal three residues of farnesylated peptides containing the CAAX motif where C is cysteine, A is an aliphatic amino acid and X is any amino acid. Cleaves the CAAX motif C-terminal to both P1 and P1' positions. Hydrolysis depends on a farnesylated cysteine residue and no activity is shown towards geranylgeranylated peptides. {ECO:0000269|PubMed:24291792}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Helix (17); Mutagenesis (8); Site (2); Topological domain (9); Transmembrane (8); Turn (2) |
| Keywords | 3D-structure;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24291792}; Multi-pass membrane protein {ECO:0000269|PubMed:24291792}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4CAD; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,197 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.7 uM for peptide substrate DABCYL-ARSGAKASGC(farnesyl)LVS-EDANS where EDANS is 5-[(2-aminoethyl)amino]naphthalene-1-sulphonic acid fluorophore and DABCYL is 4-{[4-(dimethylamino)phenyl]azo}benzoic acid quencher {ECO:0000269|PubMed:24291792}; Note=kcat is 0.175 sec(-1) for peptide substrate DABCYL-ARSGAKASGC(farnesyl)LVS-EDANS. {ECO:0000269|PubMed:24291792}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |