| IED ID | IndEnz0002014093 |
| Enzyme Type ID | protease014093 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA Dshi_1191 |
| Organism | Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodobacterales Roseobacteraceae Dinoroseobacter Dinoroseobacter shibae Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12) |
| Enzyme Sequence | MTELAAVSFVYPDLDALAAETAKIAVLVPAEGTLNPGARRLNRLTKGAVARAVESAAFEKLKSGESLSLGYPAGMASDEVILVKLARNAKPLEARKAGAGLGKTLGKEGLLIWAAGLGQVAELAFGAALRAYRFDARKSKSEDALGPITVCATKRDEAEAAFADRRAVAEGVFFTRDLVNEPANVLTTTEFADRLTAMADLGLEVSVLEEADMEKLGMGALLGVGQGSESPSKIVVMKWMGGGDGAPFALVGKGVVFDTGGISIKPSAGMEDMTMDMGGAGVVAGVMRTLALRKAKANVVGLVGLVENMPDGKAQRPGDVVTSMKGDTIEVINTDAEGRLVLADVMWYAQEEFKPCAMIDLATLTGAIIIGLGHENAGVFSNSDDLSGAFLKAATAEGEGAWRMPMGPAYDKLIKSRVADIKNVGGRAAGSITAAQFLGRFVKDETPWCHLDIAGTASVSSATDYAPAGATGWGVRALDRLIRDGYEG |
| Enzyme Length | 488 |
| Uniprot Accession Number | A8LI79 |
| Absorption | |
| Active Site | ACT_SITE 265; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 339; /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 | 50,718 |
| Kinetics | |
| Metal Binding | METAL 253; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 258; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 258; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 276; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 335; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 337; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 337; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |