| IED ID | IndEnz0002019085 |
| Enzyme Type ID | protease019085 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA CT1180 |
| Organism | Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Chlorobi Chlorobia Chlorobiales Chlorobiaceae Chlorobaculum Chlorobaculum tepidum Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) |
| Enzyme Sequence | MKCTVTAKESGLVNADILVQFFSKKEMKRDAGKVLAGLGVVASPDGDFKASAGEIAMLYRQASGKEASRVILAGVGEGKTAEDYRKAADSVARKTVDLHLGVLALDCSPIDDWAKQSKQKPEELAAILVEGVLSGAYRFDRLKSGKLDKEETKEDKPKNIEELVLAGCGSRLEAIEKGAGKGMIIGACQNRARDLVNLPGNHLSAEDLAEAAIEAGKRGGFEVTVFDKKKIVELGMGGLLAVNKGSEQPPTFVILDYKPKGKAKKTIALVGKGVTFDSGGISLKPAQGMDEMKSDMSGAAVVIAAIEAAASLGLPLRVVGLVPATDNMPGGSAQKPGDVITTMSGITVEVGNTDAEGRLILADALFYAKKEYNPDVIIDLATLTGACIVALGNSVAGLFSNDEKLAESIFEAGQSSGEKVWRLPLWDEYDELIKSDVADVHNTGGRGAGTITAAKFLEKFIDGHKHWAHIDIAGPAFWAKGGSKTPGATGFGVRLLLDLLKGWS |
| Enzyme Length | 504 |
| Uniprot Accession Number | Q8KD74 |
| Absorption | |
| Active Site | ACT_SITE 284; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 358; /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 | 52,995 |
| Kinetics | |
| Metal Binding | METAL 272; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 277; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 277; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 295; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 354; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 356; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 356; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |