| IED ID | IndEnz0002014359 |
| Enzyme Type ID | protease014359 |
| Protein Name |
Peptidyl-Asp metalloendopeptidase EC 3.4.24.33 Endopeptidase Asp-N Fragments |
| Gene Name | |
| Organism | Pseudomonas fragi |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas chlororaphis group Pseudomonas fragi |
| Enzyme Sequence | ESNQGYVNSNVGIELARYETTNYTESGSFDTDLARFRGTSDSIHTSRNTYTAADCATGYYSFAHEIGHLQSARDIATDSSTSPYAYGHGYRYEPATGWRTIMAYNCTRSCPRLNYWSNPNISYDIGPDNQRVLVNTKATIAAFR |
| Enzyme Length | 144 |
| Uniprot Accession Number | Q9R4J4 |
| Absorption | |
| Active Site | ACT_SITE 65; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds.; EC=3.4.24.33; Evidence={ECO:0000269|PubMed:2669754, ECO:0000269|PubMed:7188696}; |
| DNA Binding | |
| EC Number | 3.4.24.33 |
| Enzyme Function | FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues. {ECO:0000269|PubMed:2669754, ECO:0000269|PubMed:7188696}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (2); Non-adjacent residues (5); Non-terminal residue (1) |
| Keywords | Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,113 |
| Kinetics | |
| Metal Binding | METAL 64; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 68; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Rhea ID | |
| Cross Reference Brenda |