Detail Information for IndEnz0002018803
IED ID IndEnz0002018803
Enzyme Type ID protease018803
Protein Name Probable isoaspartyl peptidase/L-asparaginase CG7860
EC 3.4.19.5
EC 3.5.1.1
Beta-aspartyl-peptidase CG7860
Isoaspartyl dipeptidase CG7860
L-asparagine amidohydrolase CG7860

Cleaved into: Probable isoaspartyl peptidase/L-asparaginase CG7860 alpha chain; Probable isoaspartyl peptidase/L-asparaginase CG7860 beta chain
Gene Name CG7860
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MPRPVLLIHGGAGDISDSRIAGKFAGIKQALRSAWGLLSPDNGSGGGSALDAVEAAVRSMELDENFNAGYGSCLNTSGQVELEASLMEGRDLRAGCITLLRDVMHPITVARRLMEKQRHTFLGGAAAQELALATGSERLQPGALVTEGARLTLKEFEDQVAQGKDPFFARTELTDDKPVPKTDPSGETVGAVAMDASGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNCRGGVSTTGHGETLMRYNLAQRILSAMEYQGLSAQAAADKECREMTKRLGGTGGAIVVGHSGDLGISFTSRRMAWGYVQDGTIFYGIEGQVVHQEPFTLST
Enzyme Length 332
Uniprot Accession Number Q9VXT7
Absorption
Active Site ACT_SITE 188; /note=Nucleophile; /evidence=ECO:0000250
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; Evidence={ECO:0000250|UniProtKB:Q7L266}; CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266};
DNA Binding
EC Number 3.4.19.5; 3.5.1.1
Enzyme Function FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (2); Region (2)
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. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12505997; 12593804; 14605208; 17418114; 18353099; 20220848; 20371351; 21074052; 22595244; 23071443; 23972280; 25312911; 26173873; 26896675; 27346357; 28742844; 31068592; 31690598; 31722958; 33748138;
Motif
Gene Encoded By
Mass 34,861
Kinetics
Metal Binding
Rhea ID RHEA:21016
Cross Reference Brenda