IED ID | IndEnz0002018725 |
Enzyme Type ID | protease018725 |
Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
Gene Name | pepA H16_A2990 |
Organism | Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Cupriavidus Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) |
Enzyme Sequence | MEFSTKALDWSKAGQNGFLATKTDCLVVGLFEGQNLAGVAKALDVATKGLVGRLVKQGDFEGKRGTQLMLHEVAGVGAARVLLVGLGKEADFSDKAFADAVRTAVRALSSTRAASALWCLAQQAPQQRDVAWAVITTITLVREAGYRLLERHPGLKRANANGKPNGNDKSSLRKVVIAVDTGNARAATQAVVRGTAIANGMELTRDLGNLPSNICTPTYLANTARGIAKRHKLKAEVLGRKQIEALNMGAFLAVTKGSEEPPQFIVLRYDGAGAKQAPVVLVGKGITFDTGGISLKPGEGMDEMKYDMCGAASVLGTIQAVAEMGLKLNVIAVVPTCENMPSGIATKPGDVVTSMSGQTIEILNTDAEGRLILCDALTYVERFKPAAVIDVATLTGACIIALGHINSGLYARSDALADALLQAGRRAMDTAWRMPLDDEYQDQLKSNFADMGNIGGRPAGSVTAACFLSRFTEKYDWAHLDIAGTAWKSGAAKGATGRPVPLLAQFLMDRAA |
Enzyme Length | 512 |
Uniprot Accession Number | Q0K7F5 |
Absorption | |
Active Site | ACT_SITE 296; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 370; /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 | 53,988 |
Kinetics | |
Metal Binding | METAL 284; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 289; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 289; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 307; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 366; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 368; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 368; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
Rhea ID | |
Cross Reference Brenda |