| IED ID | IndEnz0002002538 |
| Enzyme Type ID | protease002538 |
| Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
| Gene Name | MAP2 LELG_04878 |
| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Enzyme Sequence | MSTDTSIKAGIDSIRAKADDLHLAEDSSNGTQANLDKHQIKATTAVGQDNGNNAGVADHKNDKNNKNNKNNNDDDDDDEDDDVAAAAAAVGDAGSDKKKKKKKSSNKKKKKKLVSIDQSYPDGVFPEGEWQEYGLDSNKYRTTSEEMRYLDRQQNNKWEDFRKGAEIHRRVRAKAKSSIRPGMTMIEIADLIENSVRAYASADHTLKAGIGFPTGLSLNHVAAHYTPNTGDKLTLGKDDLMKVDIGVHVNGRICDSAFTMTFNEDGKYDSIMQAVKEATNTGVKEAGIDVRLNDIGAAVQEVMESYEMELDGKTYPIKCIKNLNGHNIGDFIIHSGKTVPIVANGDMTKMEEGETFAIETFGSTGNGYVLPEGECSHYALNSGVESIKPPSDKAKHLLNTIQSNFGTLPWCRRYLERTGEEKYLFALNQLVKAGIVEDYPPIVDKRGSYTAQFEHTILLHPHKKEVVTRGDDY |
| Enzyme Length | 473 |
| Uniprot Accession Number | A5E5I9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 224; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 334; /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: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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Compositional bias (1); Metal binding (7); Region (1) |
| Keywords | 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,168 |
| Kinetics | |
| Metal Binding | METAL 244; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 255; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 255; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 326; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 359; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 454; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 454; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |