Detail Information for IndEnz0002002382
IED ID IndEnz0002002382
Enzyme Type ID protease002382
Protein Name Methionine aminopeptidase 2-2
MAP 2-2
MetAP 2-2
EC 3.4.11.18
Peptidase M
Gene Name AFLA_092260
Organism Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus flavus Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)
Enzyme Sequence MGSKTFEGEGQRGGNDPSNSTSPNSAGGEPRGAHLSRDGDGSLGDGDGDDGADGDEKDGAVTTTPLTEQQPSSETTSKKKKRRKPKKKISALKQSSPPRVPLDDLFPTGQFPVGETHEYGSVVEGTARTTSEEVRYLSRNYLQDDSVLTDYRKAAEIHRQVRHWTQENVRPGQTLTEIAVGIEDGVRALLDNAGLETGQCLQSGMGFPTGLALNDCVAHYTPNPGQKDIVLQASDVMKVDFGVHINGWIVDSAFTMSFDPTYDNLLAAVKDATNTGIKNAGIDVRISDVSAAIQEAMESYEVEIGGKVFPVKPVRDISGHNINRYQIHGGKSIPFVKNSSQTKMEEGEIFAIETFGSTGRGSTVEGFGVYGYGKDPNAPKKVSSPLASARSLYKTINENFGSIVFCRRYLERLGVERYLAGMNSLVNNGIVEQYAPLMDMKGSYSAQFEHTILLRESCKEVVSRGNDY
Enzyme Length 468
Uniprot Accession Number B8NLL0
Absorption
Active Site
Activity Regulation
Binding Site BINDING 219; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 328; /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 50,724
Kinetics
Metal Binding METAL 240; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 251; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 251; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 320; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 353; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 449; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 449; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda