| IED ID | IndEnz0002002401 |
| Enzyme Type ID | protease002401 |
| Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
| Gene Name | HCDG_06216 |
| Organism | Ajellomyces capsulatus (strain H143) (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 H143) (Darling's disease fungus) (Histoplasma capsulatum) |
| Enzyme Sequence | MGSKTPGNHRRDPNESSRPPAIDAINPPKQAAASGLVHGSLEGESQKRNKRKKKKKKKNTKELEILQTTPPRVALANIFRSQRYPEAEIVKYSSDNDNLQRTTAEELRHLSVLNAMDDEFLNDYRNAAEVHRQVRQYVQTIIKPGIALSQLAQEIEDGVRALTNHQGLETGDALKAGMAFPTGLCLNNIAAHWTPNPGAKEVILQYDDVLKIDFGVHVNGRIVDSAFTMAFNPVYDNLLAAVKNATNTGLKEAGIDARIAHISETIQEVMESYEVELNRKVIPVKAVRNITGHNILHYKIHGDKQVPFVKTQTNQRMEEGDVFAIETFGSTGKAYLDDATGIYGYGYDENASTAGLHHSSAKSLLKTIKENFGTLVFSRRYLERLGVQRYHLGMRSLVTNGIVQSYAPLVDVPGSYVAQFEHTVLLRPNCKEVISRGDDY |
| Enzyme Length | 440 |
| Uniprot Accession Number | C6HI66 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 192; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 301; /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 | 48,946 |
| Kinetics | |
| Metal Binding | METAL 213; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 224; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 224; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 293; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 326; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 421; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 421; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |