Detail Information for IndEnz0002002392
IED ID IndEnz0002002392
Enzyme Type ID protease002392
Protein Name Methionine aminopeptidase 2-2
MAP 2-2
MetAP 2-2
EC 3.4.11.18
Peptidase M
Gene Name NFIA_034070
Organism Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Enzyme Sequence MGSKSPEGHWQAPHASNSNELKPANPDPQTSQNGSGSADLDRGVIGDDDDDDEDAEENGVNTETPNVEKKKKRKKSNKKKKKKTKSGTLSVTELKQTSPPRVLVSTLFPSEYPVGELVPYDCTTRTTDEESRYNSRLWDDDFLPDYRQAAEIHRQVRQYAQKELIKPGATLLSIAEGIEDGVRALSGHQGLEPGDFFKAGMGFPTGLCLNHIAAHWTPNPREKDVILDKGDVLKVDFGVHVNGRIVDSAFTVAFDDKYDNLLTAVREATNTGIKHAGVDARMSDIGAAIQEVMESYEVEIDGKVFPVKAIRNITGHDILRYHIHGGKQIPFIKNNNQDKMEEGEVYAIETFGSTGRGFLDDDVGVYGYGRNENMSGANLRLSSAKSLLKTIDANFGSIVFSRRYLERLGVKNYLLGMKNLVDNGIVECYSPLVDVKGSYTAQFEHTILLHSGGKEVISRGDDY
Enzyme Length 463
Uniprot Accession Number A1CYM1
Absorption
Active Site
Activity Regulation
Binding Site BINDING 215; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 324; /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 (3); 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 51,127
Kinetics
Metal Binding METAL 236; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 247; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 247; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 316; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 349; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 444; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 444; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda