Detail Information for IndEnz0002019153
IED ID IndEnz0002019153
Enzyme Type ID protease019153
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 PYRAB02120 PAB0145
Organism Pyrococcus abyssi (strain GE5 / Orsay)
Taxonomic Lineage cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus abyssi Pyrococcus abyssi (strain GE5 / Orsay)
Enzyme Sequence MVAIIVHGGAGTIRKEERIPKVLEGVREAVLAGWKELKKGSALDAVEEAIKVLEDNPIFNAGTGSVLTIDGKVEMDAAIMRGKTLEAGAVAGIWGVKNPISVARKVMEKTDHVLLVGEGAVKFARIMGFPEYDPTTEERRKQWQELKEKLMKGEVRHWKKLGELIKEHPEVLRSTVGAVAFDGEEVVAGTSTGGVFLKMFGRVGDTPIIGAGTYANEVAGASCTGLGEVAIKLALAKTATDFVRLGLDAQAASEAAIELATKHFGKDTMGIIMVDSRGNVGFAKNTKHMSYAFMKEGMNEPEAGV
Enzyme Length 305
Uniprot Accession Number Q9V262
Absorption
Active Site ACT_SITE 175; /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;
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
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 32,591
Kinetics
Metal Binding
Rhea ID RHEA:21016
Cross Reference Brenda