| IED ID | IndEnz0002004463 |
| Enzyme Type ID | protease004463 |
| Protein Name |
Thermostable carboxypeptidase 1 EC 3.4.17.19 Carboxypeptidase Pfu PfuCP |
| Gene Name | PF0456 |
| 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 | MEEVFQNETIKQILAKYRRIWAIGHAQSVLGWDLEVNMPKEGILERSVAQGELSVLSHELLLHPEFVNLVEKAKGLENLNEYERGIVRVLDRSIRIARAFPPEFIREVSETTSLATKAWEEAKAKDDFSKFEPWLDKIISLAKRAAEYLGYEEEPYDALLDLYEEGLRTRDVEKMFEVLEKKLKPLLDKILEEGKVPREHPLEKEKYEREWMERVNLWILQKFGFPLGTRARLDVSAHPFTTEFGIRDVRITTRYEGYDFRRTILSTVHEFGHALYELQQDERFMFTPIAGGVSLGIHESQSRFWENIIGRSKEFVELIYPVLKENLPFMSNYTPEDVYLYFNIVRPDFIRTEADVVTYNFHILLRFKLERLMVSEEIKAKDLPEMWNDEMERLLGIRPRKYSEGILQDIHWAHGSIGYFPTYTIGTLLSAQLYYHIKKDIPDFEEKVAKAEFDPIKAWLREKIHRWGSIYPPKELLKKAIGEDMDAEYFVRWVKEKYL |
| Enzyme Length | 499 |
| Uniprot Accession Number | Q8U3L0 |
| Absorption | |
| Active Site | ACT_SITE 270; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P42663 |
| Activity Regulation | ACTIVITY REGULATION: EDTA and DTT reversibly abolish carboxypeptidase activity. {ECO:0000269|PubMed:10595552}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity, except for -Pro.; EC=3.4.17.19; Evidence={ECO:0000269|PubMed:10595552}; |
| DNA Binding | |
| EC Number | 3.4.17.19 |
| Enzyme Function | FUNCTION: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu. {ECO:0000269|PubMed:10595552}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90-100 degrees Celsius. {ECO:0000269|PubMed:10595552}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.2-6.6. {ECO:0000269|PubMed:10595552}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (3); Chain (1); Helix (30); Metal binding (3); Turn (4) |
| Keywords | 3D-structure;Carboxypeptidase;Cobalt;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1K9X; 1KA2; 1KA4; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 59,043 |
| Kinetics | |
| Metal Binding | METAL 269; /note=Cobalt; catalytic; /evidence=ECO:0000269|PubMed:11839307; METAL 273; /note=Cobalt; catalytic; /evidence=ECO:0000269|PubMed:11839307; METAL 299; /note=Cobalt; /evidence=ECO:0000269|PubMed:11839307 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.B5; |