Detail Information for IndEnz0002002409
IED ID IndEnz0002002409
Enzyme Type ID protease002409
Protein Name Methionine aminopeptidase 2
MAP 2
MetAP 2
EC 3.4.11.18
Peptidase M
Gene Name map-2 Y116A8A.9
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MPPANGKKGKKGGAAKAVRRIQYRPKSFKHSRFVKHAHFWSAAPEEDFDAILAEMQLADAKTAAKEATKKDAKGGKGKANGSAAATAAPEEAKQAWQAEIAAMKPIDEQFPDGKFPHGIDESPYYLKGKDGRVATDRESNEEKKALDISYEEVWQDYRRSAEAHRQVRKYVKSWIKPGMTMIEICERLETTSRRLIKEQGLEAGLAFPTGCSLNHCAAHYTPNAGDTTVLQYGDVCKIDYGIHVRGRLIDSAFTVHFDPKFDPLVEAVREATNAGIKESGIDVRLCDVGEIVEEVMTSHEVELDGKSYVVKPIRNLNGHSIAQYRIHAGKTVPIVKGGEQTKMEENEIYAIETFGSTGKGYVHDDMETSHYMKNFELADEKIPLRLQKSKGLLNLIDKNFATLAFCRRWIDRLGETKYLMALKDLCDKGIVDPYPPLCDVKGCYTAQWEHTILMRPTVKEVVSRGDDY
Enzyme Length 468
Uniprot Accession Number H1UBK1
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by the fumagillin analog, TNP-470. {ECO:0000269|PubMed:15474045}.
Binding Site BINDING 219; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 327; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
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:0000269|PubMed:15474045};
DNA Binding
EC Number 3.4.11.18
Enzyme Function FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins (PubMed:15474045). 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) (PubMed:15474045). Required for germ cell proliferation and/or differentiation (PubMed:15474045). {ECO:0000269|PubMed:15474045}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Binding site (2); Chain (1); Metal binding (7); Region (1)
Keywords Alternative splicing;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_03175}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 14551910; 15338614; 15489339; 17486083; 17704769; 17850180; 20439774; 20439776; 20610404; 21085631; 21177967; 21367940; 22267497; 22560298; 22921415; 23800452; 24884423; 25487147; 27506200; 6593563;
Motif
Gene Encoded By
Mass 52,375
Kinetics
Metal Binding METAL 239; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 250; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 250; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 319; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 352; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 449; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 449; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda