ID A0A0A0A9R3_CHAVO Unreviewed; 559 AA.
AC A0A0A0A9R3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
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};
DE Flags: Fragment;
GN ORFNames=N301_14709 {ECO:0000313|EMBL:KGL91309.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91309.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL91309.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91309.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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}.
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DR EMBL; KL871235; KGL91309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A9R3; -.
DR STRING; 50402.A0A0A0A9R3; -.
DR MEROPS; M01.004; -.
DR UniPathway; UPA00878; -.
DR Proteomes; UP000053858; 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:UP000053858};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR612777-3}.
FT DOMAIN 411..555
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT ACT_SITE 331
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT BINDING 82..84
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 214..219
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 511..513
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL91309.1"
FT NON_TER 559
FT /evidence="ECO:0000313|EMBL:KGL91309.1"
SQ SEQUENCE 559 AA; 63679 MW; 202954B02DCBDCAA CRC64;
VLDTKDVQVY KVTVNGQDAK FGFGEKHSFK GTPLEIALPF ELKRGQEAIV EISFESSPKS
SALQWFTPEQ TSGKKHPFLF SQCQATHCRA IFPCQDTPAV KLTYYAEISV PKELVALMSA
NRDGEMPDPE DSSRKIYRFS QNVPIPCYLV ALVVGALESR KIGPRTLVWA EKELVDKSAY
EFAEAEAMLK TAEDLAGPYV WGQYDLLVLP PSFPYGGMEN PCLTFVTPTL LAGDRSLSNV
IAHEISHSWT GNLVTNKTWE HFWLNEGHTV YLERRIGGRL FGEQFRHFQA LGGWRELQNT
INTLGDKNPV TNLVPNLSEV DPDVAYSSVP YEKGFALLFY LEQLLGGPDV FIGFLKAYIQ
QFAYKSIVTE DWKNFLYSYF KDKVDVLDKV DWNSWFHAPG MPPVKPKYDM TLANACVALS
QRWIKAKESD LGSFSSADLK EMSSHQLIEF LALLLLEDPL PVSHVKRMQE VYDFNAINNS
EIRFRWLRLC IKSKWEEAIP LALKMATDQG RMKFTRPLFR DLYNFDKCRD LAVKTFLEHR
ASMHPVTSML VGKDLKQDQ
//
