Detail Information for IndEnz0002002346
IED ID IndEnz0002002346
Enzyme Type ID protease002346
Protein Name Methionine aminopeptidase
MAP
MetAP
EC 3.4.11.18
Peptidase M
Gene Name map TP_0842
Organism Treponema pallidum (strain Nichols)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Spirochaetales Treponemataceae Treponema Treponema pallidum Treponema pallidum subsp. pallidum (syphilis treponeme) Treponema pallidum (strain Nichols)
Enzyme Sequence MIRIKTPEQIDGIRASCKALARLFDVLIPLVKPGVQTQELDAFCQRFIRSVGGVPAWFSEGFPAAACISINEEVIHGLPSARVIQDGDLVSLDVGINLNGYISDACRTVPVGGVAHERLELLRVTTECLRAGIKACRAGARVRAVSRAVYAVAARHRFGVVYEYCGHGVGLAVHEEPNIPNVPGLEGPNPRFLPGMVVAIEPMLTLGTDEVRTSADGWTVVTADGSCACHVEHTVAVFADHTEVLTEPTEVERTG
Enzyme Length 255
Uniprot Accession Number O83814
Absorption
Active Site
Activity Regulation
Binding Site BINDING 76; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; BINDING 174; /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 18509523;
Motif
Gene Encoded By
Mass 27,316
Kinetics
Metal Binding METAL 93; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 104; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 104; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 167; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 201; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 232; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 232; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974
Rhea ID
Cross Reference Brenda