Detail Information for IndEnz0002002347
IED ID IndEnz0002002347
Enzyme Type ID protease002347
Protein Name Methionine aminopeptidase 1
MAP 1
MetAP 1
EC 3.4.11.18
Peptidase M 1
Gene Name metap1
Organism Xenopus laevis (African clawed frog)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog)
Enzyme Sequence MAAVESRVCETEGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDDKIKPEVSPWTMDGEVNTDPWPGYRYTGKLRPHYPLTPMRPVPSYIQRPDYADHPLGMSESEQTLKGTSQIKTLSPEDIEGMRVVCRLAREVLGVAAMMVKSGITTEEIDHAVHLACISRNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQDGDIVNVDITVYRDGYHGDLNETFYVGDVDEGAKRLVETTYECLMQAIDEVKPGVRYRELGNIIQKHAQANGFSIVRSYCGHGIHKLFHTAPNVPHYGKNKAVGVMKPGHVFTIEPMICEGGWQDETWPDGWTAITRDGKRSAQFEHTLLVTETGCEILTCRLEENGRPYFIS
Enzyme Length 385
Uniprot Accession Number Q7ZWV9
Absorption
Active Site
Activity Regulation
Binding Site BINDING 203; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 301; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174
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};
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_03174}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Erroneous initiation (1); Metal binding (7); Region (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 43,196
Kinetics
Metal Binding METAL 220; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 231; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 231; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 294; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 327; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 358; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 358; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174
Rhea ID
Cross Reference Brenda