Detail Information for IndEnz0002002329
IED ID IndEnz0002002329
Enzyme Type ID protease002329
Protein Name Methionine aminopeptidase
MAP
MetAP
EC 3.4.11.18
Peptidase M
Gene Name map MG172
Organism Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Tenericutes Mollicutes Mycoplasmatales Mycoplasmataceae Mycoplasma Mycoplasma genitalium Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Enzyme Sequence MIYLKSANEVAGIKKACAIFKAVKAYFTIEKLLGKKLVTIDRLIKQFIEQKQAKCAFHGYLGFPGFNCLSLNQTVIHGVADQTVFKDSDKLTLDIGIDYHGYLCDAAFTLLGNKADPKAVKLLNDVEQAFSKVIEPELFVNNPIGNLSNAIQTYFENKGYFLVKEFGGHGCGIKIHEDPLILNWGEKNQGVRLQEGMVICIEPMVMTDSSEITMAANNWNVLTLKSKFNCHVEQMYHITNNGFECLTN
Enzyme Length 248
Uniprot Accession Number P47418
Absorption
Active Site
Activity Regulation
Binding Site BINDING 77; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; BINDING 176; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
DNA Binding
EC Number 3.4.11.18
Enzyme Function FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-Rule:MF_01974}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 27,738
Kinetics
Metal Binding METAL 94; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 105; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 105; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 169; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 202; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 233; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 233; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974
Rhea ID
Cross Reference Brenda