| IED ID | IndEnz0002016749 |
| Enzyme Type ID | protease016749 |
| Protein Name |
Cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP Leucyl aminopeptidase Proline aminopeptidase EC 3.4.11.5 Prolyl aminopeptidase |
| Gene Name | ECU10_1770i |
| Organism | Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Microsporidia Apansporoblastina Unikaryonidae Encephalitozoon Encephalitozoon cuniculi (Microsporidian parasite) Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
| Enzyme Sequence | MELLSYEKLMIGDELNKDSVKVRIVLCSNSKEGVGIMADEKSPGHQNFLSRLDAKGHVGEAYVLLEGNGEVTVFVGIGNVEEDILLVKNNARKAGASAYKCVSQFKNMEMSLTSEYMAREVVSGIMLASYKYRFLHKEKDEPSKKIAINSQSHAVKKAVVVGNAQNFARFLGDTPANLMNPTLFVEYATKYLQDKKNVTFEVFDKSFMERKSMNLLLGVSQGSAQEPKLLVARYRGKSGDAVDIALVGKGVCFDSGGISLKPSARMHRMKGDMLGAASVLSVFGLAADMGIKINMNLVIPLVENLPSGTATKPGDVHVGMNGKSVEINNTDAEGRLILADALVYAQEANPTYIVDVATLTGAMMIALGDAFIGYFTADDDLSKIIHQSGIDANDPVWRMPLSQLYLPSMKSNVADLKNAVEGGHGGSATAAIFLSEFVGKEFKWAHFDIAGVMDSNNNKGVYGDGATGCGVPVLIEMIEKLSTIIN |
| Enzyme Length | 486 |
| Uniprot Accession Number | Q8SQZ7 |
| Absorption | |
| Active Site | ACT_SITE 261; /evidence=ECO:0000250; ACT_SITE 335; /evidence=ECO:0000250 |
| 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; CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.5 |
| 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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,389 |
| Kinetics | |
| Metal Binding | METAL 249; /note=Zinc 2; /evidence=ECO:0000250; METAL 254; /note=Zinc 1; /evidence=ECO:0000250; METAL 254; /note=Zinc 2; /evidence=ECO:0000250; METAL 272; /note=Zinc 2; /evidence=ECO:0000250; METAL 331; /note=Zinc 1; /evidence=ECO:0000250; METAL 333; /note=Zinc 1; /evidence=ECO:0000250; METAL 333; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |