Detail Information for IndEnz0002002356
IED ID IndEnz0002002356
Enzyme Type ID protease002356
Protein Name Methionine aminopeptidase 2-1
MAP 2-1
MetAP 2-1
EC 3.4.11.18
Peptidase M
Gene Name AFUB_018820
Organism Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Enzyme Sequence MGSKSPEGHRQAPHASNCNELKPANPDPQISQNGSGSADLDRGVIGDDDDDEDAEENGVNTETPNVGKLNQPPFPNLDQVHVTTTDGLCITEKKKKRKKSNKKKKKTKSGALPATELKQTSPPRVLVSTLFPSEYPVGELVPYDCTARTTDEELRYNSRLWDDDFLPDYRQAAEIHRQVRQYAQKELIKPGATLLSIAEGIEDGVRALSGHQGLEPGDFFKAGMGFPTGLCLNHIAAHWTPNPREKDVILDKGDVLKVDFGVHVNGRIVDSAFTVAFDDKYDNLLTAVREATNTGIKHAGVDARMSDIGAAIQEVMESYEVEIDGKVFPVKAIRNITGHDILRYHIHGGKQIPFIKNNNQDKMEEGEVYAIETFGSTGRGFLDDDVGVYGYGRNENMSGANLRLSSAKSLLKTIDASFGSIVFSRRYLERLGVKNYLLGMKNLIDNGIVECYSPLVDVKGSYTAQFEHTILLHSGGKEVISRGDDY
Enzyme Length 486
Uniprot Accession Number B0XTJ7
Absorption
Active Site
Activity Regulation
Binding Site BINDING 238; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 347; /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 (4); 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_03175}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 53,508
Kinetics
Metal Binding METAL 259; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 270; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 270; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 339; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 372; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 467; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 467; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda