| IED ID | IndEnz0002002530 |
| Enzyme Type ID | protease002530 |
| Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
| Gene Name | MAP2 ECU10_0750 |
| Organism | Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Microsporidia Apansporoblastina Unikaryonidae Encephalitozoon Encephalitozoon cuniculi (Microsporidian parasite) Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
| Enzyme Sequence | MKCILLNQAEELPIEFLPKDGVYGKGKLFDSRNMEIENFTESDILQDARRAAEAHRRARYRVQSIVRPGITLLEIVRSIEDSTRTLLKGERNNGIGFPAGMSMNSCAAHYTVNPGEQDIVLKEDDVLKIDFGTHSDGRIMDSAFTVAFKENLEPLLVAAREGTETGIKSLGVDVRVCDIGRDINEVISSYEVEIGGRMWPIRPISDLHGHSISQFRIHGGISIPAVNNRDTTRIKGDSFYAVETFATTGKGSIDDRPPCSHFVLNTYKSRKLFNKDLIKVYEFVKDSLGTLPFSPRHLDYYGLVKGGSLKSVNLLTMMGLLTPYPPLNDIDGCKVAQFEHTVYLSEHGKEVLTRGDDY |
| Enzyme Length | 358 |
| Uniprot Accession Number | Q8SR45 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 109; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; BINDING 218; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503" |
| 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_03175}; |
| DNA Binding | |
| EC Number | 3.4.11.18 |
| Enzyme Function | FUNCTION: Cotranslationally 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). {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14736176, ECO:0000269|PubMed:16004378, ECO:0000269|PubMed:16917013}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:19660503}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:19660503}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (12); Binding site (2); Chain (1); Helix (9); Metal binding (7); Mutagenesis (1); Natural variant (1); Turn (2) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3FM3; 3FMQ; 3FMR; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,975 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.95 mM for a Met-Ala-Ser peptide {ECO:0000269|PubMed:19660503}; Vmax=7.3 nmol/min/mg enzyme {ECO:0000269|PubMed:19660503}; |
| Metal Binding | METAL 130; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; METAL 141; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; METAL 141; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; METAL 210; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; METAL 243; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; METAL 339; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503"; METAL 339; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:19660503" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.18; |