| IED ID | IndEnz0002016628 |
| Enzyme Type ID | protease016628 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA pc1103 |
| Organism | Protochlamydia amoebophila (strain UWE25) |
| Taxonomic Lineage | cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Parachlamydiales Parachlamydiaceae Candidatus Protochlamydia Candidatus Protochlamydia amoebophila Protochlamydia amoebophila (strain UWE25) |
| Enzyme Sequence | MEFALTLHIEKRKKADVLVLPFWKGTSQPEAAIALHPLKLSLDSVFNTGDFKGKEGETLFLYVEGLVEMRVALLGLGEKNKVSTEALRKSYGCLAKACLGKKLKTLNILMPEFNKTEEDAFIKAITEGLLLPNYVYDRLKSKQEEDDEVTLLQKINFISSNKHVLALAEEVAAICDGVYYTRDLINGNADEITPQYLAKCAQGLSQEYPQIKTTVFDKKRLEKEQMGLLLAVNRGSNLDPTLIIMEYKGNPKSKDHTVIIGKGVTYDTGGLNIKPTGGIETMKCDMSGGAACFGTMLAACHLDLKVNLTAIIPATENSVDAASFKPGDVYRSYLGKTVEMTNSDAEGRLILADALAYASQNLKPSRLIDIATLTGAIEISLGSEASGLMSTDDQLAKSLIQAGENTHERLWRMPLYEGYQEKLKSDIADLKSWNGRSGSSCVAAMFLKNFVGKDIPWAHLDIAGTAYVTEPKKYMPKYASGVGVRLLVEFLKQLSMVKN |
| Enzyme Length | 499 |
| Uniprot Accession Number | Q6MC72 |
| Absorption | |
| Active Site | ACT_SITE 274; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 348; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.10 |
| Enzyme Function | FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,776 |
| Kinetics | |
| Metal Binding | METAL 262; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 267; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 267; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 285; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 344; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 346; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 346; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |