| IED ID | IndEnz0002016556 |
| Enzyme Type ID | protease016556 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA Avin_11650 |
| Organism | Azotobacter vinelandii (strain DJ / ATCC BAA-1303) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Azotobacter group Azotobacter Azotobacter vinelandii Azotobacter vinelandii (strain DJ / ATCC BAA-1303) |
| Enzyme Sequence | MQLVVKSTSPQTLKTATLVVAVGEGRKLGATAKAIDQAADGALSAALKRGDLAGKVGQTLLLHAVPNLKAERVLLVGAGKEGELSDRQFRKIAAATYGALKGLGGSDAALTLGELQVKGRDTYGKTRLLAETLLDATYAFDRFKSEKASAPVLKKLVLLCDKAGQAEVERAASHAQAIVDGMALTRDLGNLPPNLCHPTSLASEAKALAKTYDTLKVEVLDEKKLKELGMGAFLAVAQGSDQPPRLIVLDYQGGKKDEQPFVLVGKGITFDSGGISLKPGSGMDEMKYDMCGAASVLGTFRALLELALPINVVGLLACAENMPSGGATRPGDIVTSMSGQTVEILNTDAEGRLVLCDALTYAERFKPQAVIDIATLTGACITALGTQASGLMGNDDDLIRQVLEAGEHAADRAWQLPLFEEYQEQLDSPFADMANIGGPKAGTITAACFLSRFAKNYHWAHLDIAGTAWISGGKEKGATGRPVPLLTQFLLDRSAP |
| Enzyme Length | 496 |
| Uniprot Accession Number | C1DPG2 |
| Absorption | |
| Active Site | ACT_SITE 278; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 352; /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 |
| 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 | 52,115 |
| Kinetics | |
| Metal Binding | METAL 266; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 271; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 271; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 289; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 348; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 350; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 350; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |