| IED ID | IndEnz0002000289 |
| Enzyme Type ID | protease000289 |
| Protein Name |
Xaa-Pro dipeptidase X-Pro dipeptidase EC 3.4.13.9 Imidodipeptidase Proline dipeptidase Prolidase |
| Gene Name | pepQ AHA_0141 |
| Organism | Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Aeromonadales Aeromonadaceae Aeromonas Aeromonas hydrophila Aeromonas hydrophila subsp. hydrophila Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) |
| Enzyme Sequence | MSSYSQLFAQHLDTLQQRTRDILQQQGLSGLAIHSGQTHRIFLDDQDYPFKVNPQFKAWLPVLDNPHCWLLVDGVNKPVLLFYRPVDFWHKVAELPNAFWVDFFDIRFLTRPEQVADHLPANKQEWAYLGGHLEVAELLGLGQPNPEAVLNYLHYHRAYKTAYELECLRDANRIGVRGHIAAKDSFMAGASEFEINLAYMKAVGQGANEAPYGNIVAINRNAAILHYTHLSAQRVPDAERYSFLIDAGVDVHGYASDITRTWAWRRGEFADLIAALDAQQQEIIEEIKPGRRYSELHLQMHHRLARLLQATELVDMSVDEMIHTGVTNVFFPHGLGHFLGLQVHDAGGFMQDERGTHLSAPEQFPYLRCTRVMEVGQVFTIEPGLYFIDSLLEPLRLGEQGKRVNWNKVEALRPYGGIRIEDNVVLHANGVENLTRQAGL |
| Enzyme Length | 440 |
| Uniprot Accession Number | A0KEL3 |
| 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; Evidence={ECO:0000255|HAMAP-Rule:MF_01279}; |
| DNA Binding | |
| EC Number | 3.4.13.9 |
| Enzyme Function | FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal position. {ECO:0000255|HAMAP-Rule:MF_01279}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (7) |
| Keywords | Dipeptidase;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,049 |
| Kinetics | |
| Metal Binding | METAL 246; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01279; METAL 257; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01279; METAL 257; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01279; METAL 337; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01279; METAL 382; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01279; METAL 421; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01279; METAL 421; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_01279 |
| Rhea ID | |
| Cross Reference Brenda |