| IED ID | IndEnz0002016784 |
| Enzyme Type ID | protease016784 |
| Protein Name |
Putative L-asparaginase EC 3.5.1.1 L-asparagine amidohydrolase Cleaved into: Putative L-asparaginase subunit alpha; Putative L-asparaginase subunit beta |
| Gene Name | TK2246 |
| Organism | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Thermococcus Thermococcus kodakarensis Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Enzyme Sequence | MAAIIVHGGAGTIRKEERIPKVIEGVREAVLAGWRELKRGSALDAVEEAVKALEDNPIFNAGTGSVLTLDGKVEMDAAIMRGKTLDAGAVAGIWGVKNPISVARKVMEKTDHVLLIGEGAVKFARLLGFEEYDPITEERLKQWEELRKKLIEKGETKHWKKLNELIKEYPEVLRSTVGAVAFDGEEVVAGTSTGGVFLKMFGRVGDTPIIGGGTYANEVAGASCTGLGEVAIKLALAKSAADFVRLGMDAQTASEAAISLATKYFGPDTMGIIMVDAKGNVGFAKNTKHMSYAFMKDGMDEPEAGV |
| Enzyme Length | 306 |
| Uniprot Accession Number | Q5JHT1 |
| Absorption | |
| Active Site | ACT_SITE 176; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P37595 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; |
| DNA Binding | |
| EC Number | 3.5.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Region (2); Site (1) |
| Keywords | Autocatalytic cleavage;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,642 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21016 |
| Cross Reference Brenda | 3.5.1.1; |