IED ID | IndEnz0002002574 |
Enzyme Type ID | protease002574 |
Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
Gene Name | MAP2 YBL091C YBL0701 |
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 | MTDAEIENSPASDLKELNLENEGVEQQDQAKADESDPVESKKKKNKKKKKKKSNVKKIELLFPDGKYPEGAWMDYHQDFNLQRTTDEESRYLKRDLERAEHWNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGAENLLAMEDPKSQGIGFPTGLSLNHCAAHFTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEINGETYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEDHQVMPTLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSKGDDY |
Enzyme Length | 421 |
Uniprot Accession Number | P38174 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Irreversibly inhibited by the fungal metabolite fumagillin, an antiangiogenic drug. Subject to product inhibition by cytosolic methionine. {ECO:0000269|PubMed:12874831, ECO:0000269|PubMed:9177176}. |
Binding Site | BINDING 174; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 282; /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, ECO:0000269|PubMed:8618900}; |
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 only a minor role in N-terminal methionine removal. Less efficient when the second residue is Val, Gly, Cys or Thr. {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:11811952, ECO:0000269|PubMed:12874831, ECO:0000269|PubMed:15547949, ECO:0000269|PubMed:8618900, ECO:0000269|PubMed:9177176}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Compositional bias (1); Erroneous initiation (1); Metal binding (7); Modified residue (1); Mutagenesis (1); Region (1); Sequence conflict (2) |
Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Phosphoprotein;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14562095}. |
Modified Residue | MOD_RES 35; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10515904; 10727764; 11805837; 14676204; 14690591; 15210064; 16386852; 16917013; 17229726; 18719252; 19536198; 21655302; 22093065; 22350874; 26195668; 26456335; 9367524; |
Motif | |
Gene Encoded By | |
Mass | 47,518 |
Kinetics | |
Metal Binding | METAL 194; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 205; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 205; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 274; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 307; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 402; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 402; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Rhea ID | |
Cross Reference Brenda |