Detail Information for IndEnz0002002368
IED ID IndEnz0002002368
Enzyme Type ID protease002368
Protein Name Methionine aminopeptidase 2-1
MAP 2-1
MetAP 2-1
EC 3.4.11.18
Peptidase M
Gene Name Pc14g00010
Organism Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium rubens Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Enzyme Sequence MGSKTAENESQGGGNAPPSSTKATATGGEPRGAHWSRDGDGTLGEGEGDDDADGDNTSCAPAVPLNPQTAPSTNSKKRKKRPKKKTSALKQSSPPRIPLADLFPDHQYPHGEAQVYEPGLENVARTTADEVRHHSRHHIEDDTFLNDYRKAAEVHRQVRRWTQESVRPGQTLTEIAMGIEDGVRALLDNAGLDTGQGLISGLGFPTGLSLNNCVAHYTPNPGQREVVLDSSDVMKVDFGVHINGWIVDSAFTMSFDPTYDNLLAAVKDATNTGIKNAGVDVRISDVSAAIQEAMESYEVDINGRTFPVKAVRNITGHNIEQYRIHAGKSIPFVKNNDNTKMEEGEIFAIETFGTTGRGYLFDGPGVYGYGKDPSAPKRITSHLASAKSLYQKINENFGSLVFCRRYLERLGVESYLAGMNNLVSNGYVEVYQPLMDVRGSYSAQFEHTILLRESCKEVISRGDDY
Enzyme Length 465
Uniprot Accession Number B6H5L5
Absorption
Active Site
Activity Regulation
Binding Site BINDING 216; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 325; /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 50,739
Kinetics
Metal Binding METAL 237; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 248; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 248; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 317; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 350; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 446; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 446; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda