| IED ID | IndEnz0002000119 |
| Enzyme Type ID | protease000119 |
| Protein Name |
Peptidase B EC 3.4.11.23 Aminopeptidase B |
| Gene Name | pepB PC1_3024 |
| Organism | Pectobacterium carotovorum subsp. carotovorum (strain PC1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Pectobacterium Pectobacterium carotovorum (Erwinia carotovora) Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) Pectobacterium carotovorum subsp. carotovorum (strain PC1) |
| Enzyme Sequence | MTNNTMLISLSTQPADARWGEKATLSVNEQGFTIHVGTTSLNGKAALATIQRAARKIDGQGIKHVKLAGEGWDLANSWAFWQGYRGPKGQRTVEWADLSDADKKELNDRLKIVDWVRDTINLPAEDLGPEQLATRAVDLLCDVACDAISYRITKGEDLREQNYAGLHTVGRGSERQPVLLALDYNPTGNADAPVFACLVGKGITFDTGGYSLKPSSSMDSMKSDMGGAATLTGALALAASRGLQQRVKLYLCCADNMVSGNAFRLGDIIRYRNGKTVEVMNTDAEGRLVLADGLIDASEQNPQWIIDCATLTGAAKMALGNDYHALFSFDDELVAALQESAKEENEPFWRLPLEEFHRSHLPSSFADLNNIASGANTAGASTAAAFLSHFVKNYQQGWLHIDCSATYRKSAVEQWATGATGLGVRTLANLLLSNAK |
| Enzyme Length | 436 |
| Uniprot Accession Number | C6DBI4 |
| Absorption | |
| Active Site | ACT_SITE 213; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; ACT_SITE 287; /evidence=ECO:0000255|HAMAP-Rule:MF_00504 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln.; EC=3.4.11.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00504}; |
| DNA Binding | |
| EC Number | 3.4.11.23 |
| Enzyme Function | FUNCTION: Probably plays an important role in intracellular peptide degradation. {ECO:0000255|HAMAP-Rule:MF_00504}. |
| 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_00504}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,133 |
| Kinetics | |
| Metal Binding | METAL 201; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; METAL 206; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; METAL 206; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; METAL 224; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; METAL 283; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; METAL 285; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00504; METAL 285; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00504 |
| Rhea ID | |
| Cross Reference Brenda |