Detail Information for IndEnz0002002550
IED ID IndEnz0002002550
Enzyme Type ID protease002550
Protein Name Methionine aminopeptidase 2
MAP 2
MetAP 2
EC 3.4.11.18
Peptidase M
Gene Name MAP2 PGUG_05790
Organism Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Meyerozyma Meyerozyma guilliermondii (Yeast) (Candida guilliermondii) Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Enzyme Sequence MAKTRTNSETVSILHTLHTNQKAPGARVYRVFRFSHHPKMRSNMSQDKEANEIAVNTTETVVSTPTDVTTAETKTDGSPETNAAPAAAKKKKNKKKKKITSIDSSYPDGVFPEGEWQEYPLEINSYRTSSEELRYLDNQRNNHWQDFRKGAEIHRRVRHKAQSSIRPGMTMTEIADLIENSVRSYAAADHTLKAGIGFPTGLSLNEIAAHYTPNAGDKLVLGKDDVMKVDIGVHVNGHIVDSAFTMTFDDDHKYDNLLKAVKEATNTGVREAGIDVRLNDIGAAVQEVMESYEMEIGGKTYPIKCIRNLNGHNIGDYVIHSGKTVPIVANGDMTKMEEGETFAIETFGSTGNGYVIPTGECSHYALSEEYKQARVGTDRAKQLLKTIESNFGTLPWCRRYLDRVGEEKYLLALNQLVRAGAVQDYPPITDRAGSYTAQFEHTILLHPHKKEVVSRGDDY
Enzyme Length 459
Uniprot Accession Number A5DR89
Absorption
Active Site
Activity Regulation
Binding Site BINDING 210; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 320; /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 51,166
Kinetics
Metal Binding METAL 230; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 241; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 241; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 312; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 345; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 440; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 440; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda