| IED ID | IndEnz0002018790 |
| Enzyme Type ID | protease018790 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA ROP_08760 |
| Organism | Rhodococcus opacus (strain B4) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Nocardiaceae Rhodococcus Rhodococcus opacus (Nocardia opaca) Rhodococcus opacus (strain B4) |
| Enzyme Sequence | MSTRTARPLGPQLALAGTVGKRVDVLVIGLTSSSDGPEIALGDGIVDEAVLTGLLDTLVAVGASGKAEETTRIPAPDTLPVDSVLAVGLGSAEKLDAEQIRKSAGAAARTLSGVGTAATTLSVLDLGAAAEGFALGAYRFTEFKSAKSAPGPDAQPVARVELLVSSPRAKESKDTLARSAAIAEAVATAREFVNTPPSHLFPAEFADRAKELGTDSGLKVEVLDEKALEKNGYGGILGVGKGSSRLPRLVRLSYSAKKRNAPKVALVGKGITFDTGGISIKPAAGMENMTSDMGGAAAVVATVVLAAKLGLPVDVTATVPMAENMPSSTAQRPGDVLTQYGGTTVEVINTDAEGRLVLADAIVRACEDDPDYLIDTATLTGAQMVALGNRTPGVMGTDAFRDRVAAISQEIGENAWAMPMPAELRSDLDSKIADLANVTNHRWGGMLAAALYLKEFVADGVQWAHIDVAGPAYNSSGPWGYTGRGGTGVPVRTMISVIEDIAAHG |
| Enzyme Length | 505 |
| Uniprot Accession Number | C1AUB5 |
| Absorption | |
| Active Site | ACT_SITE 281; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 355; /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 |
| 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 | 51,824 |
| Kinetics | |
| Metal Binding | METAL 269; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 274; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 274; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 292; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 351; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 353; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 353; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |