| IED ID | IndEnz0002002335 |
| Enzyme Type ID | protease002335 |
| Protein Name |
Methionine aminopeptidase 1 MAP 1 MetAP 1 EC 3.4.11.18 Peptidase M 1 |
| Gene Name | fma1 SPBC3E7.10 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MATEIAKHICCGIDCNNEADRLQCPKCLNDGVKSYFCGQECFRNSWNIHKHLHRPPNVEKREDGTYNPFPKFHFAGSLKPVYPLSPIRKVPPHIKRPDYAKTGVSRSEQIEGRSFKLKRLTPKEQEGMRKVCRLGREVLDAAAAAVRPGTTTDELDSIVHNACIERDCFPSTLNYYAFPKSVCTSVNEIICHGIPDQRPLEDGDIVNIDVSLYHNGFHGDLNETYYVGDKAKANPDLVCLVENTRIALDKAIAAVKPGVLFQEFGNIIEKHTNSITEKQISVVRTYCGHGINQLFHCSPSIPHYSHNKAPGIARPGMTFTIEPMLTLGPARDITWPDDWTSSTASGRCSAQFEHTLLVTETGCEVLTARLPNSPGGPLK |
| Enzyme Length | 379 |
| Uniprot Accession Number | O59730 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 192; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 296; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| 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_03174}; |
| 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_03174}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Metal binding (7); Modified residue (1); Region (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Phosphoprotein;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. |
| Modified Residue | MOD_RES 373; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16491466; 18684775; 20473289; 23697806; 24763107; 29996109; 30647105; 30726745; 32062975; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,139 |
| Kinetics | |
| Metal Binding | METAL 209; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 220; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 220; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 289; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 322; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 353; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 353; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| Rhea ID | |
| Cross Reference Brenda |