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Database: UniProt
Entry: A0A3Q3N4F8_9TELE
LinkDB: A0A3Q3N4F8_9TELE
Original site: A0A3Q3N4F8_9TELE 
ID   A0A3Q3N4F8_9TELE        Unreviewed;       599 AA.
AC   A0A3Q3N4F8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Leukotriene A4 hydrolase {ECO:0000313|Ensembl:ENSMAMP00000031437.2};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000031437.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000031437.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   AlphaFoldDB; A0A3Q3N4F8; -.
DR   Ensembl; ENSMAMT00000032256.2; ENSMAMP00000031437.2; ENSMAMG00000021165.2.
DR   GeneTree; ENSGT00940000156375; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004463; F:leukotriene-A4 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; 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; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634015-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT   DOMAIN          459..589
FT                   /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT                   C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01263"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        380
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         129..131
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT   BINDING         263..268
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT   BINDING         292
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         545..547
FT                   /ligand="a peptide"
FT                   /ligand_id="ChEBI:CHEBI:60466"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ   SEQUENCE   599 AA;  68282 MW;  4097B67B6BA19D0E CRC64;
     FDERLEIKTG CVTKHLNLSF HLDFDRHIIR GKVELTVEAL EDRFSALTLD TKDLKIISAL
     ANGQPARFSL GPKHSFKGTP LDITLPFEIS RGQHVIVEVT YETSTSASAL QWLTPEQTAG
     KKQPYLFSQC QAHHCRSMVP CQDSPSVKHT YYAQVSVPKD LVAVMSAMRD GQEDDPQDSN
     RTIYRFRQPV GVLFLPSVYC ITIVITCSRE IGPRSRVWSE KEFVDKAAFE FSETETMLKT
     AEDLVGPYVW GQYDILVLPP SFPYGGMENP CLTFATPTLL AGDKSLSDVI AHEISHSWTG
     NLVTNKTWEH FWLNEGHTVY LERMIGRCMK SEQFRQFDAI GGWKDLQDSV NTFGANNPLT
     NLVPSLQDVD PDDAFSSVPY EKGFALLYHL EELMGGPEVF MGFVKSYIQM FAYSSVTTEE
     WKNYLFTYFK DKVNILKKVD WNAWMFTPVM KPPSFAPLQA KDQDLSSFKK SDVKVLSSQQ
     LTEFLSLLLH EDPLPLSHVK KMQEVYDLNA YMNSEIRFRW LRLCVRSRWE EAVPTALKMA
     TEQGRMKFTR PLFREVYNFE KYRDEAVRVF LASQAAMHPV TSGLVAKDLK VGASNTTSL
//
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