IED ID | IndEnz0002000340 |
Enzyme Type ID | protease000340 |
Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 Imidodipeptidase Proline dipeptidase Prolidase |
Gene Name | pepQ PH1149 |
Organism | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus horikoshii Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
Enzyme Sequence | MDIMNEKVKKIIEFMDKNSIDAVLIAKNPNVYYISGASPLAGGYILITGESATLYVPELEYEMAKEESNIPVEKFKKMDEFYKALEGIKSLGIESSLPYGFIEELKKKANIKEFKKVDDVIRDMRIIKSEKEIKIIEKACEIADKAVMAAIEEITEGKKEREVAAKVEYLMKMNGAEKPAFDTIIASGYRSALPHGVASDKRIERGDLVVIDLGALYQHYNSDITRTIVVGSPNEKQKEIYEIVLEAQKKAVESAKPGITAKELDSIARNIIAEYGYGEYFNHSLGHGVGLEVHEWPRVSQYDETVLREGMVITIEPGIYIPKIGGVRIEDTILITKNGSKRLTKTERELI |
Enzyme Length | 351 |
Uniprot Accession Number | O58885 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9; |
DNA Binding | |
EC Number | 3.4.13.9 |
Enzyme Function | FUNCTION: Splits dipeptides with a prolyl in the C-terminal position and a nonpolar amino acid at the N-terminal position. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (18); Chain (1); Helix (12); Metal binding (7); Turn (1) |
Keywords | 3D-structure;Cobalt;Cytoplasm;Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1WY2; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 39,401 |
Kinetics | |
Metal Binding | METAL 212; /note=Cobalt 2; METAL 223; /note=Cobalt 1; METAL 223; /note=Cobalt 2; METAL 287; /note=Cobalt 1; METAL 316; /note=Cobalt 1; METAL 330; /note=Cobalt 1; METAL 330; /note=Cobalt 2 |
Rhea ID | |
Cross Reference Brenda | 3.4.13.9; |