Detail Information for IndEnz0002002332
IED ID IndEnz0002002332
Enzyme Type ID protease002332
Protein Name Methionine aminopeptidase
MAP
MetAP
EC 3.4.11.18
Peptidase M
Gene Name map RP824
Organism Rickettsia prowazekii (strain Madrid E)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rickettsiales Rickettsiaceae Rickettsieae Rickettsia typhus group Rickettsia prowazekii Rickettsia prowazekii (strain Madrid E)
Enzyme Sequence MTIKIHTEKDFIKMRAAGKLAAETLDFITDHVKPNVTTNSLNDLCHNFITSHNAIPAPLNYKGFPKSICTSINHVVCHGIPNDKPLKNGDIVNIDVTVILDGWYGDTSRMYYVGDVAIKPKRLIQVTYDAMMKGIEVVRPGAKLGDIGYAIQSYAEKHNYSVVRDYTGHGIGRVFHDKPSILNYGRNGTGLTLKEGMFFTVEPMINAGNYDTILSKLDGWTVTTRDKSLSAQFEHTIGVTKDGFEIFTLSPKKLDYPPY
Enzyme Length 259
Uniprot Accession Number Q9ZCD3
Absorption
Active Site
Activity Regulation
Binding Site BINDING 78; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974"; BINDING 176; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.3"; BINDING 220; /note="Substrate"; /evidence="ECO:0000269|Ref.3"
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 (13); Binding site (3); Chain (1); Helix (6); Metal binding (7); Turn (2)
Keywords 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 3MR1; 3MX6;
Mapped Pubmed ID 28089350;
Motif
Gene Encoded By
Mass 28,861
Kinetics
Metal Binding METAL 95; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"; METAL 106; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"; METAL 106; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"; METAL 169; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"; METAL 202; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"; METAL 234; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"; METAL 234; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|Ref.2, ECO:0000269|Ref.3"
Rhea ID
Cross Reference Brenda 3.4.11.18;