ID A0A3B3WPU1_9TELE Unreviewed; 614 AA.
AC A0A3B3WPU1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Leukotriene A(4) hydrolase {ECO:0000256|RuleBase:RU361141};
DE Short=LTA-4 hydrolase {ECO:0000256|RuleBase:RU361141};
DE EC=3.3.2.6 {ECO:0000256|RuleBase:RU361141};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000004815.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000004815.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene A4 = leukotriene B4; Xref=Rhea:RHEA:22324,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57461, ChEBI:CHEBI:57463; EC=3.3.2.6;
CC Evidence={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 -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004716, ECO:0000256|RuleBase:RU361141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU361141}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU361141}.
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DR RefSeq; XP_014841320.1; XM_014985834.1.
DR AlphaFoldDB; A0A3B3WPU1; -.
DR STRING; 48701.ENSPMEP00000004815; -.
DR Ensembl; ENSPMET00000008535.1; ENSPMEP00000004815.1; ENSPMEG00000006111.1.
DR GeneID; 106917104; -.
DR KEGG; pmei:106917104; -.
DR CTD; 4048; -.
DR OrthoDB; 443480at2759; -.
DR UniPathway; UPA00878; -.
DR Proteomes; UP000261480; 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:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
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 Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751,
KW 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR612777-3}.
FT DOMAIN 460..604
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:PIRSR612777-1"
FT ACT_SITE 380
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT BINDING 131..133
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 263..268
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 560..562
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
SQ SEQUENCE 614 AA; 69842 MW; 1108FBC596CF7B36 CRC64;
MSDPCSFSSF STCLTKHLNL QLHVDFDRHV IRGKVQLTVE ALEDRFSVLT LDSRDLNVSS
VSVNQQTAHY ELGPKHSFKG TPLVITLPFD LSRGQQVIVE VTYETSPSAF ALQWLTPEQT
AGKKQPYLFS QCQAHHCRSM IPCQDTPSIK HTYYAQVSVP KQLVAVMSAV RDGQEVDPQD
TGRIVYRFRQ PVAMPSYLIA IVVGALESRE IGPRSRVWSE MEFVDKAASE FSETETMLKT
AEDLAGPYVW GQYDVLVLPP SFPYGGMENP CLTFATPTLL AGDKSLSGVI AHEISHSWTG
NLVTNRTWEH FWLNEGHTVY LERMIGRRME GEQFRQFKAI GGWKDLQDSV NTFGANNPLT
NLVPSLQEVN PDDAFSSVPY EKGFALLYHL EELMGGPEVF MGFVKSYIQR FAYSSVTTDD
WKSYLFTYFK DKVDILNKVD WKGWMFTPGM PPVKPQYDTT LADACIALTQ RWIKAKDQDL
NVFSQSDVKT LSSHQLIEFL SLLLQEEPLP LSHVKRMQEV YDLNASTNSE IRFRWLRLCV
RCQWEEAVPL ALKMATEQGR MKFTRPLFRE VFNFEKYREE AVRVFLAHRA AMHPVTSGLV
AKDLKVDASS TGDR
//
