| IED ID | IndEnz0002016009 |
| Enzyme Type ID | protease016009 |
| Protein Name |
Isoaspartyl peptidase EC 3.4.19.5 Beta-aspartyl-peptidase Isoaspartyl dipeptidase Cleaved into: Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta |
| Gene Name | iaaA STM0847 |
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
| Enzyme Sequence | MNKAVIAIHGGAGAIARAQMSHEQELRYIQALSEIVESGQKMLEAGDSALDVVTEAVRLLEACPLFNAGIGAVYTRDGTHELDACVMDGNTLKAGAVAGVSHVRHPVLAARLVMERSPHVLMVGEGAENFAFSQGMARVSPDIFSTPARYEQLLAARAAGEMALDHSGAPLDETKKMGTVGAVARDKFGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRTLAAYDIAALMEYGGLSLADACERVVMEKLPALGGSGGLIAVDHEGNVALPFNSEGMYRAWGYAGDTPTTGIYRE |
| Enzyme Length | 313 |
| Uniprot Accession Number | Q7CQV5 |
| Absorption | |
| Active Site | ACT_SITE 179; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; |
| DNA Binding | |
| EC Number | 3.4.19.5 |
| Enzyme Function | FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and tripeptides. Acts best on iso-Asp-Leu, followed by iso-Asp-Ala, -His and to a lesser extent iso-Asp-Lys, -Phe and iso-Asp-Leu-Ala. Does not act on internal iso-Asp bonds (Als-iso-Asp-Leu-Ala). Does not act on alpha-Asp bonds. Has poor L-asparaginase activity. {ECO:0000269|PubMed:11325937}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2); Site (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Autocleaved. Generates the alpha and beta subunits. The beta subunit is thought to be responsible for the nucleophile hydrolase activity. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,473 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |