| IED ID | IndEnz0002002371 |
| Enzyme Type ID | protease002371 |
| Protein Name |
Methionine aminopeptidase 2-1 MAP 2-1 MetAP 2-1 EC 3.4.11.18 Peptidase M |
| Gene Name | PMAA_027380 |
| Organism | Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces marneffei (Penicillium marneffei) Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei) |
| Enzyme Sequence | MAAQASEELEKLKLNGQNGHAQEQVSAADEAADNDDSEDDEKEEEGGAEGAATGAAKKKKKRKPKKKKKGGAKKQSSPPRVPISELFPNNQYPEGEIVEYKDENNYRTTNEEKRYLDRMNNDFLQEYRHGAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDAVRALTGHQGLEEGDNIKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAHINGRIVDSAFTMTFDPVYDNLLAAVKDATNTGIREAGIDVRMSDIGAAIQEAMESYEVEINGTTYPVKAIRNLNGHNIEQHIIHGGKSVPIVKGGDQTKMEEGEVFAIETFGSTGKGYVRDDMETSHYAKVSNAPSVSLRLSSAKNLLNVINKNFGTLPFCRRYLDRLGQDKYLLGLNNLVSAGIIQDYPPLCDIKGSYTAQYEHTIVLRPTVKEIISRGDDY |
| Enzyme Length | 442 |
| Uniprot Accession Number | B6Q1N3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 195; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 303; /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 (2); 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 | 48,696 |
| Kinetics | |
| Metal Binding | METAL 215; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 226; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 226; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 295; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 328; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 423; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 423; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |