ID A0A2Y9MGF9_DELLE Unreviewed; 611 AA.
AC A0A2Y9MGF9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
GN Name=LTA4H {ECO:0000313|RefSeq:XP_022418112.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022418112.1};
RN [1] {ECO:0000313|RefSeq:XP_022418112.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022418112.1};
RG RefSeq;
RL Submitted (NOV-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_022418112.1; XM_022562404.1.
DR AlphaFoldDB; A0A2Y9MGF9; -.
DR STRING; 9749.A0A2Y9MGF9; -.
DR Ensembl; ENSDLET00000016881; ENSDLEP00000015275; ENSDLEG00000011258.
DR KEGG; dle:111168728; -.
DR InParanoid; A0A2Y9MGF9; -.
DR OrthoDB; 443480at2759; -.
DR UniPathway; UPA00878; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004301; F:epoxide hydrolase activity; IEA:Ensembl.
DR GO; GO:0004463; F:leukotriene-A4 hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR612777-3}.
FT DOMAIN 464..608
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT ACT_SITE 384
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT BINDING 135..137
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 267..272
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
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 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 564..566
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
SQ SEQUENCE 611 AA; 69263 MW; 049553BF6106DF1A CRC64;
MPEVVDTCSL ASPASVCRTK HLHLRCSVDF TRRVLTGTAA LTVQSQEDNL RSLILDTKDL
TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALCKNQE IVIEISFETS PKSSALQWLT
PEQTSGKEHP YLFSQCQAIH CRAVLPCQDT PSVKLTYSSE VSVPKELVAL MSAIRDGEAP
DPEDASRKIY RFSQKVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES
MLKIAEDLGG PYIWGQYDLL VLPPSFPYGG MEHPCLTFVT PTLLAGDKSL SNVIAHEISH
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FHALGGWGEL QNSIKTFGET
HPFTKLVVDL TNVDPDVAYS SVPYEKGFAL LFYLEQLLGG PEVFLGFLKA YVEKFSYKSI
TTDDWKDFLY SHFKDKVDIL NQVDWNAWLY SPGLPPVKPN YDMTLTNACI ALSQRWITGK
EDDLNSFSSA DLKDFSSHQV NEFLAQMLQK APLPLGHIKR MQEVYNFNAI NNSEIRFRWL
RLCIQSKWEE AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAIRTYQ EHKACMHPVT
AMLVGKDLKV D
//
