Detail Information for IndEnz0002003298
IED ID IndEnz0002003298
Enzyme Type ID protease003298
Protein Name Putative aminopeptidase FrvX
EC 3.4.11.-
Gene Name frvX yiiI b3898 JW3869
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MNIELLQQLCEASAVSGDEQEVRDILINTLEPCVNEITFDGLGSFVARKGNKGPKVAVVGHMDEVGFMVTHIDESGFLRFTTIGGWWNQSMLNHRVTIRTHKGVKIPGVIGSVAPHALTEKQKQQPLSFDEMFIDIGANSREEVEKRGVEIGNFISPEANFACWGEDKVVGKALDNRIGCAMMAELLQTVNNPEITLYGVGSVEEEVGLRGAQTSAEHIKPDVVIVLDTAVAGDVPGIDNIKYPLKLGQGPGLMLFDKRYFPNQKLVAALKSCAAHNDLPLQFSTMKTGATDGGRYNVMGGGRPVVALCLPTRYLHANSGMISKADYEALLTLIRGFLTTLTAEKVNAFSQFRQVD
Enzyme Length 356
Uniprot Accession Number P32153
Absorption
Active Site ACT_SITE 205; /note=Proton acceptor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.11.-
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (6)
Keywords Aminopeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11544210; 16606699; 9473030;
Motif
Gene Encoded By
Mass 38,733
Kinetics
Metal Binding METAL 61; /note=Divalent metal cation 1; /evidence=ECO:0000250; METAL 175; /note=Divalent metal cation 1; /evidence=ECO:0000250; METAL 175; /note=Divalent metal cation 2; /evidence=ECO:0000250; METAL 206; /note=Divalent metal cation 2; /evidence=ECO:0000250; METAL 228; /note=Divalent metal cation 1; /evidence=ECO:0000250; METAL 316; /note=Divalent metal cation 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda