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
//