Detail Information for IndEnz0002002188
IED ID IndEnz0002002188
Enzyme Type ID protease002188
Protein Name Leucine aminopeptidase 2
EC 3.4.11.-
Epoxide hydrolase
EC 3.3.2.10
Leukotriene A-4 hydrolase homolog
LTA-4 hydrolase
Gene Name MGG_09481
Organism Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae) Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Enzyme Sequence MAARDPSTASNYDAWKTKHTTANLRIDFDDKCLRGSVVLELESRTAKESKEIVLDSSYVSVESIKLNDVQTKWEIKERNGPMGSPLHISVPEGADSGEVVRLEMAVKTTPQCTALQWLTPAQTSNKKAPFMFSQAQACHARSLFPCQDTPDVKSTYSFNITSPHVVVASGVANDGDKAEADGGDKVYKYEQNVPIPSYLFALASGDIAMAPIGPRSSVATGPDEVKECQWELEEDMGKFMDAAERLVFPYKWGEYNVLVLPPSFPYGGMENPIYTFATPTIISGDRQNTDVIAHELSHSWSGNLVTSCSWEHYWLNEGWTMYLERRIIAAVRGPAYFDFSALLGWKHLEDAIEEFGADHKFTQLCINHKGIDPDDAFSTVPYEKGFHMVYYLDRLVGRKNFDKFIPYYFTKWANKSLDSYEFKDTFLEFFDKPEYADLKDKIAGIDWEGRFYTPGLPPKPEFDTSLVDVCYALADKWKKGDYTPSSKDVDGWTGNQKLVFLGSVQDFEQPLSAEQAKQLGNAYDLIETKNVELKTAYYLIALRAQDSTAYQGVADLLGQVGRMKFVRPLFRALNKVDRPLALTTFEKNKDFYHPICRAMAEKDLGLSDDAKKE
Enzyme Length 613
Uniprot Accession Number A4QUC1
Absorption
Active Site ACT_SITE 295; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 382; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:Q10740};
DNA Binding
EC Number 3.4.11.-; 3.3.2.10
Enzyme Function FUNCTION: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro). {ECO:0000250|UniProtKB:Q10740}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Erroneous initiation (1); Metal binding (3); Region (2)
Keywords Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10740}. Nucleus {ECO:0000250|UniProtKB:Q10740}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 69,113
Kinetics
Metal Binding METAL 294; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 298; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 317; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID RHEA:19037
Cross Reference Brenda