ID   LKHA4_MAGO7             Reviewed;         613 AA.
AC   A4QUC1; G4N1U6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Leucine aminopeptidase 2;
DE            EC=3.4.11.-;
DE   AltName: Full=Epoxide hydrolase;
DE            EC=3.3.2.10;
DE   AltName: Full=Leukotriene A-4 hydrolase homolog;
DE            Short=LTA-4 hydrolase;
GN   ORFNames=MGG_09481;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Aminopeptidase that preferentially cleaves di- and
CC       tripeptides. Also has low epoxide hydrolase activity (in vitro). Can
CC       hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially
CC       5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine
CC       leukotriene B(4) as the product compared to the homologous mammalian
CC       enzyme (in vitro). {ECO:0000250|UniProtKB:Q10740}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594;
CC         EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:Q10740};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q10740};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q10740};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10740}. Nucleus
CC       {ECO:0000250|UniProtKB:Q10740}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHA52461.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CM001233; EHA52461.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_003712268.1; XM_003712220.1.
DR   AlphaFoldDB; A4QUC1; -.
DR   SMR; A4QUC1; -.
DR   STRING; 318829.MGG_09481T0; -.
DR   MEROPS; M01.034; -.
DR   PRIDE; A4QUC1; -.
DR   GeneID; 2680552; -.
DR   KEGG; mgr:MGG_09481; -.
DR   eggNOG; KOG1047; Eukaryota.
DR   InParanoid; A4QUC1; -.
DR   OrthoDB; 775595at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004301; F:epoxide hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09599; M1_LTA4H; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 1.25.40.320; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR   InterPro; IPR034015; M1_LTA4H.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR45726; PTHR45726; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..613
FT                   /note="Leucine aminopeptidase 2"
FT                   /id="PRO_0000324932"
FT   ACT_SITE        295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        382
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         134..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   613 AA;  69113 MW;  BEBAAE0845A646A0 CRC64;
     MAARDPSTAS NYDAWKTKHT TANLRIDFDD KCLRGSVVLE LESRTAKESK EIVLDSSYVS
     VESIKLNDVQ TKWEIKERNG PMGSPLHISV PEGADSGEVV RLEMAVKTTP QCTALQWLTP
     AQTSNKKAPF MFSQAQACHA RSLFPCQDTP DVKSTYSFNI TSPHVVVASG VANDGDKAEA
     DGGDKVYKYE QNVPIPSYLF ALASGDIAMA PIGPRSSVAT GPDEVKECQW ELEEDMGKFM
     DAAERLVFPY KWGEYNVLVL PPSFPYGGME NPIYTFATPT IISGDRQNTD VIAHELSHSW
     SGNLVTSCSW EHYWLNEGWT MYLERRIIAA VRGPAYFDFS ALLGWKHLED AIEEFGADHK
     FTQLCINHKG IDPDDAFSTV PYEKGFHMVY YLDRLVGRKN FDKFIPYYFT KWANKSLDSY
     EFKDTFLEFF DKPEYADLKD KIAGIDWEGR FYTPGLPPKP EFDTSLVDVC YALADKWKKG
     DYTPSSKDVD GWTGNQKLVF LGSVQDFEQP LSAEQAKQLG NAYDLIETKN VELKTAYYLI
     ALRAQDSTAY QGVADLLGQV GRMKFVRPLF RALNKVDRPL ALTTFEKNKD FYHPICRAMA
     EKDLGLSDDA KKE