| IED ID | IndEnz0002014145 |
| Enzyme Type ID | protease014145 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA Sde_1372 |
| Organism | Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Cellvibrionales Cellvibrionaceae Saccharophagus Saccharophagus degradans Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) |
| Enzyme Sequence | MEFIAKKADIATLSTQCVVVFCKDGKLMASASHLDTEQHGLLTHQLSIKAISPTAGSHLWLTLAPTKSAKHSKALLVQLGESKKKSADITIEDIRKISQKLASTLNSAKLKDAAVFFDSALPASGDCTLEKLAHTLALEIERASYRFSLKAGTKNTPATLKKVVFVATNSAETKTLRNGANTGSAMGKGINAARELGNLPGNICTPNYLAEQAKQLAAGCKKLTSKALGEKQMERLGMGAFLSVSKGSDQEGKLILLEYKGAAANKAPHVLVGKGVTFDTGGISLKPGANMDEMKFDMCGAASVLGTFKALVELDAKVNVVGIIAAAENMPSGGASKPGDVVTSMSGQTIEILNTDAEGRLVLCDALTYAERYKPKSVVDIATLTGACVVALGNHAAGLYSNTQSVADALLKAGEETHDRAWQMPLWDDYQRQLDSNFADMGNIGGMPGGSITAACFLSRYTKKYPWAHLDIAGVAWHSGAKKGATGRPVSLLVNYLLNN |
| Enzyme Length | 500 |
| Uniprot Accession Number | Q21KZ5 |
| Absorption | |
| Active Site | ACT_SITE 286; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 360; /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 | 52,731 |
| Kinetics | |
| Metal Binding | METAL 274; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 279; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 279; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 297; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 356; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 358; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 358; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |