Detail Information for IndEnz0002002574
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