ID A0A060WBS5_ONCMY Unreviewed; 615 AA.
AC A0A060WBS5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-NOV-2023, entry version 33.
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 ORFNames=GSONMT00071290001 {ECO:0000313|EMBL:CDQ64461.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ64461.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ64461.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ64461.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR904473; CDQ64461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WBS5; -.
DR STRING; 8022.A0A060WBS5; -.
DR MEROPS; M01.004; -.
DR PaxDb; 8022-A0A060WBS5; -.
DR UniPathway; UPA00878; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR612777-3}.
FT DOMAIN 463..607
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT ACT_SITE 383
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT BINDING 134..136
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 266..271
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 563..565
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
SQ SEQUENCE 615 AA; 69789 MW; E95CEEDDB590140F CRC64;
MASATDPCSF SSFSKCVTKH LNLTYHVDFD SHVIKAKVAL TVEVLVDNFT SLTLDTKDLK
VSKVTANGQA AKFTLGPKHS FMGTPLEITL PFDLSRGQHV IVEVTYETAP SASALQWLTP
EQTAGKKHPY LFSQCQATHC RSMVPCQDTP AMKHTYYAQV SVPKELVAVM SAVRDGQEPD
PQDSSRAIYR FRQPVPMPSY LIAIVVGALE SREIGPRSRV WSEKEFVDKA AFEFSETETM
LKTAEDLAGP YVWGQYDILV LPPSFPYGGM ENPCLTFATP TLLAGDRSLS NVIAHEISHS
WTGNLVTNKT WEHFWLNEGH TVYLERMIGR SMESEQFRQF KAMGGWKDLQ ESVNTFGANN
PLTNLVPNMN EVDPDDAFSS VPYEKGFALL YHLEELMGGP EVFMGFVKSY IQMFAYSSIT
TEEWKKYLFT YFKNKVDILN KVDWNAWMHT PGMPPVKPQY DTTMADACIA LCKRWVKTKE
GDLGNFSEVD MKTLSTHQLI EFLSLLLQED PLPLSHVKRM QEVYRLNALN NAEIRFRWLR
LCVKSKWEDA VPMALKMATE QGRMKFTRPL FKEVYNFDKY REEAVRVFIA HRAAMHPVTS
NLVAKDLKVD TGKST
//
