| IED ID | IndEnz0002002349 |
| Enzyme Type ID | protease002349 |
| Protein Name |
Methionine aminopeptidase 1 MAP 1 MetAP 1 EC 3.4.11.18 Peptidase M 1 |
| Gene Name | MAP1 YLR244C L9672.12 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSTATTTVTTSDQASHPTKIYCSGLQCGRETSSQMKCPVCLKQGIVSIFCDTSCYENNYKAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILTARNKKSPGGPRQRIK |
| Enzyme Length | 387 |
| Uniprot Accession Number | Q01662 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: In contract to the MetAP 2 isoform, is not inhibited by the fungal metabolite fumagillin, an antiangiogenic drug. {ECO:0000269|PubMed:9177176}. |
| Binding Site | BINDING 202; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 301; /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). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11811952, ECO:0000269|PubMed:11968008, ECO:0000269|PubMed:12874831, ECO:0000269|PubMed:7862096}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (1); Mutagenesis (3); Propeptide (1); Region (1) |
| Keywords | Acetylation;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22814378 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10224104; 10515904; 10727764; 12144506; 14563547; 14676204; 15210064; 15547949; 16386852; 16554755; 16917013; 17229726; 18205808; 18719252; 18998772; 19536198; 20934449; 21124907; 21655302; 21936842; 22350874; 2246265; 23586741; 25710965; 26195668; 26335097; 26777405; 27693354; 7644482; 8618900; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,373 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.68 mM for a Met-Ala-Ser peptide {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096}; KM=6.56 mM for a Met-Gly-Met-Met peptide {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096}; KM=139 uM for a Met-Ala-Ser-Trp peptide {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096}; Note=kcat is 1173, 1416 and 507 min(-1) with a Met-Ala-Ser, a Met-Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.; |
| Metal Binding | METAL 219; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 230; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 230; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 294; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 327; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 358; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 358; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| Rhea ID | |
| Cross Reference Brenda |