| IED ID | IndEnz0002002388 |
| Enzyme Type ID | protease002388 |
| Protein Name |
Methionine aminopeptidase 2-2 MAP 2-2 MetAP 2-2 EC 3.4.11.18 Peptidase M |
| Gene Name | GLRG_10223 |
| Organism | Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Glomerellaceae Colletotrichum Colletotrichum graminicola species complex Colletotrichum graminicola (Maize anthracnose fungus) (Glomerella graminicola) Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) |
| Enzyme Sequence | MAAQVPTEALKELNVGGPATNDKAANPTEGNGVDHDSDDSDEEGEEVAAPAAGGAAKKKKKNKKKKKKKSPTAQSDPPRVLMSSLFPNKNYPKGQEEEYRDENLYRTTNEEKRHLDNLNNDFLTDYREAAEIHRQVRQWAQKNIKPGQTLTEIAEGIEDGVRALTGHPGIEEGDAYKGGMGFPCGLSLNHCAAHYTPNAGNKMVLSQGDVMKVDFGVHVNGRIVDSAFTMAFEPQYDNLLAAVKDATNAGVKEAGIDVRVGDVGGVIQEVMESYEVEIDGTTYPVKSIRNLNGHTIERWSIHGTKSVPIVKSNDTTKMEEGDVFAVETFGSTGNGFVREDMEVSHYAKRGEGHAALRLDSAKRLLNVINKNFGTLPFCRRYLDRLGQDKYLLGLNNLVSSGIVEAYPPLCDKKGSYTAQFEHTILLRPTVKEVISRGDDY |
| Enzyme Length | 440 |
| Uniprot Accession Number | E3QW41 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 194; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 302; /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 | 48,286 |
| Kinetics | |
| Metal Binding | METAL 214; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 225; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 225; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 294; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 327; /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 |