Detail Information for IndEnz0002002364
IED ID IndEnz0002002364
Enzyme Type ID protease002364
Protein Name Methionine aminopeptidase 2-1
MAP 2-1
MetAP 2-1
EC 3.4.11.18
Peptidase M
Gene Name AN4404
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MAAQASEKLEKLDLNGQNGESAAGPAKAGQADAGEVEDESDDDADDAGAAADGAANGAAKKKKKRKSKKKKKGGAKVQSSPPRVPVSSLFANGQYPEGEIVEYKNENSYRTTNEEKRYLDRMNNDFLQEYRQGAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDSVRALTGHQGLEEGDNIKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAHINGRIVDSAFTMSFDPVYDPLLEAVKDATNTGIRSLQEAGIDVRMSDIGAAIQETMESYEIELNGTTYPIKPIRNLNGHNIDQHVIHGGKSVPIVKGSDQTKMEEGEVFAIETFGSTGKGYVREDMETSHYALVANAPQVPLRLSSAKSLLNVINKNFGTLPWCRRYLDRLGQDKYLLGLNNLVQSGIVQDYPPLCDIKGSYTAQFEHTIVLRPTVKEVISRGDDY
Enzyme Length 448
Uniprot Accession Number Q5B4X6
Absorption
Active Site
Activity Regulation
Binding Site BINDING 198; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 309; /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 48,898
Kinetics
Metal Binding METAL 218; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 229; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 229; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 301; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 334; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 429; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 429; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda