LKHA4_ASPTN
ID LKHA4_ASPTN Reviewed; 617 AA.
AC Q0CFY9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
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=ATEG_06861;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU32245.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAU32245.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH476603; EAU32245.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001209547.1; XM_001209547.1.
DR AlphaFoldDB; Q0CFY9; -.
DR SMR; Q0CFY9; -.
DR STRING; 341663.Q0CFY9; -.
DR MEROPS; M01.034; -.
DR EnsemblFungi; EAU32245; EAU32245; ATEG_06861.
DR GeneID; 4319230; -.
DR eggNOG; KOG1047; Eukaryota.
DR OrthoDB; 775595at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; IPR012777; LTA4H.
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 TIGRFAMs; TIGR02411; leuko_A4_hydro; 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..617
FT /note="Leucine aminopeptidase 2"
FT /id="PRO_0000324922"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 388
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 271..276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 617 AA; 69701 MW; F0BC113CF9551639 CRC64;
MATTINPPRD PNTLSNYNNW LSTHITANFD ILFDQKKLVG NVIHKLKSIT NAESTDIVLD
TSHVDVTDVK VDGKPSVWEL LPPVKPYGTA LKIKLDQGVK MDEIVHVDIS VKTTEKCTAL
QWLTPAQTSN KKHPYMFSQC QAIHARSIFP CQDTPDVKST IDFNITSPLP VIASGLLVRD
ASGAPQTGGK NLYQFHQKVP IPSYLFALAS GDISEAAIGP RSVVATSPDK LRECQWELEA
DTENFINAIE KIVYPYVWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENVDVIAH
ELAHSWSGNL VTNASWEHFW LNEGWTVYLE RRILAAVHGE AYRHFSAIIG WKALSDSVDH
FGHDHEFTRL ITDLKGKDPD DAFSSIPYEK GFNFLFHLEN LVGKQKFDQF IPHYFTKFKG
KSLDSYEFKA TILDFFKSDA EASKLLNELD WDTWFYAPGL PPKPKFDTSL VDVVYDLAKK
WQSIPESSFK PQPSDIKDLT GNQIVVFLEQ VLLFERPLAP ELSKLMGEVY GLAKSANIEV
ANLYFRVGLN AGDESVFEPT ADLLGKIGRM KFVRPLYRNL QKVNRPLAIE TFEKNKDFYH
PICRAMVEKD LFGKKDA
