| IED ID | IndEnz0002018578 |
| Enzyme Type ID | protease018578 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA Rmet_2807 |
| Organism | Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Cupriavidus Cupriavidus metallidurans Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) |
| Enzyme Sequence | MEFSTKALDLSKAGQNGFLATKTDCLVVGLFEGQSLAGVAKALDVATKGLVARLVKQGDFEGKRGTQLMLHEVAGVGAARVLLVGLGKEADFNDKAFAEAVRTATRALGGTRAASALWCLVQQPPQQRDVAWAIITTITLVREAGYRLLERHPELKRAPRGAGANEKASLRKIVLAVDVGDAKAASQAAVRGTAIANGMELTRDLGNLPSNICTPTYLANTARGIAKRHKLKVEILGRKQIEALNMGAFLAVTKGSVEPPQFIVLRYDGASAKQAPVVLVGKGITFDTGGISLKPGEGMDEMKYDMCGAASVLGTIQAVAEMGLKQNVIAVVPTCENMPSGIATKPGDVVTSMSGQTIEILNTDAEGRLILCDALTYVERFKPAAVIDVATLTGACIIALGHVNSGLYARSDALADQLLGAGRKAMDTAWRLPLDDDYQDQLKSNFADMANIGGRPAGSVTAACFLARYTEKYDWAHLDIAGTAWKSGAAKGATGRPVPLLTQFLMDRAA |
| Enzyme Length | 510 |
| Uniprot Accession Number | Q1LJJ6 |
| Absorption | |
| Active Site | ACT_SITE 294; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 368; /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 | 53,736 |
| Kinetics | |
| Metal Binding | METAL 282; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 287; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 287; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 305; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 364; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 366; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 366; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |