Detail Information for IndEnz0002002339
IED ID IndEnz0002002339
Enzyme Type ID protease002339
Protein Name Methionine aminopeptidase
MAP
MetAP
EC 3.4.11.18
Peptidase M
Gene Name map SAV1888
Organism Staphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain Mu50 / ATCC 700699)
Enzyme Sequence MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEYGAISAPIHDENFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNGYYADTGISFVVGESDDPMKQKVCDVATMAFENAIAKVKPGTKLSNIGKAVHNTARQNDLKVIKNLTGHGVGLSLHEAPAHVLNYFDPKDKTLLTEGMVLAIEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTKDGPILTTKIEEE
Enzyme Length 252
Uniprot Accession Number P0A078
Absorption
Active Site
Activity Regulation
Binding Site BINDING 76; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; BINDING 175; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"
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 Beta strand (10); Binding site (2); Chain (1); Helix (5); Metal binding (7)
Keywords 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Protease
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1QXW; 1QXY; 1QXZ;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 27,502
Kinetics
Metal Binding METAL 93; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 104; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 104; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 168; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 202; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 233; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"; METAL 233; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:14998322"
Rhea ID
Cross Reference Brenda