| 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 |