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Database: UniProt
Entry: A0A1L9VLY7_ASPGL
LinkDB: A0A1L9VLY7_ASPGL
Original site: A0A1L9VLY7_ASPGL 
ID   A0A1L9VLY7_ASPGL        Unreviewed;       616 AA.
AC   A0A1L9VLY7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Leukotriene A(4) hydrolase {ECO:0000256|RuleBase:RU361141};
DE            Short=LTA-4 hydrolase {ECO:0000256|RuleBase:RU361141};
DE            EC=3.3.2.10 {ECO:0000256|RuleBase:RU361141};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU361141};
GN   ORFNames=ASPGLDRAFT_124252 {ECO:0000313|EMBL:OJJ84939.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ84939.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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:0000256|ARBA:ARBA00002142}.
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:0000256|ARBA:ARBA00001268,
CC         ECO:0000256|RuleBase:RU361141};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR612777-3,
CC         ECO:0000256|RuleBase:RU361141};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR612777-3,
CC       ECO:0000256|RuleBase:RU361141};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU361141}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU361141}.
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DR   EMBL; KV878895; OJJ84939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9VLY7; -.
DR   STRING; 1160497.A0A1L9VLY7; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_124252; -.
DR   OrthoDB; 443480at2759; -.
DR   Proteomes; UP000184300; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09599; M1_LTA4H; 1.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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   NCBIfam; TIGR02411; leuko_A4_hydro; 1.
DR   PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 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; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361141};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361141};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR612777-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU361141};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR612777-3}.
FT   DOMAIN          469..610
FT                   /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT                   C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01263"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT   ACT_SITE        388
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT   BINDING         139..141
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT   BINDING         271..276
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT   BINDING         568..570
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
SQ   SEQUENCE   616 AA;  69996 MW;  F0EBABB8C0AB8D33 CRC64;
     MATIINSPRD PNTLSNYNNW ISTHITANFD ILFDQKKLAG NVVHQLKSIT DAQSQDIILD
     VNHLDIGDVK VDGKQSQWEL LPPLESYGTA LKIKLGHAVK LNETIEVDIS VKTTEKCTAL
     QWLTPAQTSN KKYPYMFSQC QAIHARSIFP CQDTPDVKST LDFNITSPHP VIASGLPVRD
     LPPALQPDGK SLYRFHQTVP IPSYLFALAS GDISEATIGP RSVVATSPDK VEECKWELEA
     DTEKFINAIE KIVYNYAWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENVDVIAH
     ELAHSWSGNL VTNASWEHFW LNEGWTTYLE RRILGAVHGE PYRHFSAIIG WKALSDSVEH
     FGQDHEFTKL VIDLKGKDPD DAFSSIPYEK GFNFLFQLET LLGKAKFDEF IPHYFTVFKE
     KSLDSYEFKT TILDFFQSDP EASKLLNDLD WDKWFYAPGL PPKPHFDTSL VDVVYELARK
     WQSLPESSFK PQASDIHGLT ANQLIVFLEQ VLLFEQLKPD LTKLMGEVYG LSKSENIEVA
     NLYFQVGLKA GDKSVLEPTA SLLSRIGRMK FVRPLYRNLQ KVNRTLAIET FEKNRDFYHP
     ICRAMVEKDL FGKKEN
//
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