| IED ID | IndEnz0002002267 |
| Enzyme Type ID | protease002267 |
| Protein Name |
Methionine aminopeptidase 1 MAP 1 MetAP 1 EC 3.4.11.18 Peptidase M 1 |
| Gene Name | METAP1 KIAA0094 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARPHFMSQF |
| Enzyme Length | 386 |
| Uniprot Accession Number | P53582 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 203; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; BINDING 301; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" |
| 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_03174, ECO:0000269|PubMed:17114291}; |
| 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). Required for normal progression through the cell cycle. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:17114291}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (15); Binding site (2); Chain (1); Erroneous initiation (2); Helix (8); Initiator methionine (1); Metal binding (7); Modified residue (1); Region (1); Turn (2) |
| Keywords | 3D-structure;Acetylation;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
| Interact With | O76003; Q0VD86; Q6FHY5; Q14596-2; Q58EX7; Q9UGI0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:19413330 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (36) |
| Cross Reference PDB | 2B3H; 2B3K; 2B3L; 2G6P; 2GZ5; 2NQ6; 2NQ7; 4FLI; 4FLJ; 4FLK; 4FLL; 4HXX; 4IKR; 4IKS; 4IKT; 4IKU; 4IU6; 4U1B; 4U69; 4U6C; 4U6E; 4U6J; 4U6W; 4U6Z; 4U70; 4U71; 4U73; 4U75; 4U76; 5YKP; 5YR4; 5YR5; 5YR6; 5YR7; 6LZB; 6LZC; |
| Mapped Pubmed ID | 12144506; 15231748; 17353931; 17636946; 17929833; 19898482; 20379614; 20521764; 22913487; 23507151; 23634668; 23767698; 25699713; 26496610; 27542228; 30837307; 32764695; 34329997; 7644482; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,215 |
| Kinetics | |
| Metal Binding | METAL 220; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; METAL 231; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; METAL 231; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; METAL 294; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; METAL 327; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; METAL 358; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291"; METAL 358; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.18; |