Detail Information for IndEnz0002002402
IED ID IndEnz0002002402
Enzyme Type ID protease002402
Protein Name Methionine aminopeptidase 2
MAP 2
MetAP 2
EC 3.4.11.18
Peptidase M
Gene Name HCAG_08694
Organism Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Ajellomycetaceae Histoplasma Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum) Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum)
Enzyme Sequence MGSKTPGNHRRGPNESSPHPAIDAINPPKQAAASRLVHSSLEGESEGGEDEDDDKPGADLKAVGQIGNNGQKRNKRRKKKKKNTKELEILQTTPPRVALANIFRSQRYPEAEIVKYSTDNDNLQRTTAEELRHISVLNAMDDEFLNDYRKAAEVHRQVRQYVQTIIKPGIALSQLAEEIEDGVRALTNHQGLETGDALKAGMAFPTGLCLNNIAAHWTPNPGAKEVILKYDDVLKIDFGVHVNGRIVDSAFTIAFNPVYDNLLAAVKDATNAGLKEAGIDARIAHISETIQNVMESYEVELNQKVIPVKAVRNITGHNVLHYKIHGDKQVPFVKTQTNQRMEEGDVFAIETFGSTGKAYLDDATGIYGYGYDENASTAGLHHSSAKSLLKTIKENFGTLVFSRRYLERLGVQRYHLGMRSLVTNGIVQSYAPLVDVPGSYVAQFEHTVLLRPNCKEVISRGDDY
Enzyme Length 464
Uniprot Accession Number A6RGC8
Absorption
Active Site
Activity Regulation
Binding Site BINDING 216; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 325; /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); 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 51,306
Kinetics
Metal Binding METAL 237; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 248; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 248; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 317; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 350; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 445; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 445; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda