| IED ID | IndEnz0002014342 |
| Enzyme Type ID | protease014342 |
| Protein Name |
Probable isoaspartyl peptidase/L-asparaginase 3 EC 3.4.19.5 L-asparagine amidohydrolase 3 Cleaved into: Isoaspartyl peptidase/L-asparaginase 3 subunit alpha; Isoaspartyl peptidase/L-asparaginase 3 subunit beta |
| Gene Name | At5g61540 K11J9.7 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MARSDVLIFVSTLLLFLSLLTVADAELVKSDKFPVVVSTWPFLEAVRAAWRAVDNGSSAVEAVVEGCSACEELRCDGTVGPGGSPDENGETMIDALVMDGVTMEVGAVAAMRYVKDGIRAAHLVMKYSQHTLLAGEGASAFAISMGLPGPMNLSSPESVKKWSDWKENQCQPNFRKNVVPANDCGPYKPNNSAMNVFVDKSTESCEMGAIEYKPPLVGPHNHDTISMAVIDRMGHIAVGTSTNGATYKIPGRVGDGPIVGSSAYADDEVGGCGATGDGDTMMRFLPCYQVVESMRQGMKPEEAAKDAISRIARKFPDFVGAVVAVDKNGSHAGACYGWTFQYSVQNPDMNDVQVFTVLP |
| Enzyme Length | 359 |
| Uniprot Accession Number | Q56W64 |
| Absorption | |
| Active Site | ACT_SITE 224; /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: Acts in asparagine catabolism but also in the final steps of protein degradation via hydrolysis of a range of isoaspartyl dipeptides. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (2); Erroneous gene model prediction (1); Region (2); Site (1) |
| Keywords | Alternative splicing;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 | 12185496; 16705405; 16941220; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,249 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |