| IED ID | IndEnz0002002552 |
| Enzyme Type ID | protease002552 |
| Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
| Gene Name | PGTG_16374 |
| Organism | Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL) (Black stem rust fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Pucciniomycotina Pucciniomycetes Pucciniales (rusts) Pucciniaceae Puccinia Puccinia graminis (Black stem rust fungus) Puccinia graminis f. sp. tritici Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL) (Black stem rust fungus) |
| Enzyme Sequence | MTIPVPKPAHPAAPDTNTDGLPNPKVVVPVEADEEEDDDDEEGKEDADGAVPAASHFSTHALDGTKKKKKKKKKPKKKKTGEAGAGGQSEPPRVPVSKLFPNGNYPSGEESAYLGENSYRTTSSEKRELERLAAQEDPESAENYNSIRRAAEVHRQVRRYVQQTVKPGMSMTEIAEMVEDGTRALVEVDGLQRGIGFPTGVSLNHCAAHYTPNAGDTIVLSADDVLKVDFGVQIGGRIVDSAFTMTFNNKYDKLLEAVRAATNTGIREAGIDARLSDIGASIQETMESYEVEVDGKVHKVKSIRNLTGHNILPYHIHGGKSVPIVANSDESAIMEEGDHFAVETFGSTGRGYVMDDGECSHYAKNPDVNKPIRLARAKTLLNTINKHFDTLPFCKRYLDRLGESRYYAALDNLVNLGIVQAYPPLSDIQGCMTAQYEHTIILRPTCKEVVSRGDDY |
| Enzyme Length | 456 |
| Uniprot Accession Number | E3L3Q8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 209; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 317; /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 | 49,884 |
| Kinetics | |
| Metal Binding | METAL 229; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 240; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 240; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 309; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 343; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 437; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 437; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
| Rhea ID | |
| Cross Reference Brenda |