ID A0A1B0FIM4_GLOMM Unreviewed; 808 AA.
AC A0A1B0FIM4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY003663-PA, ECO:0000313|Proteomes:UP000092444};
RN [1] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG International Glossina Genome Initiative W.H.O.;
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:GMOY003663-PA}
RP IDENTIFICATION.
RC STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY003663-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU361141}.
CC Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU361141}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000256|ARBA:ARBA00006227}.
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DR EMBL; CCAG010006996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0FIM4; -.
DR STRING; 37546.A0A1B0FIM4; -.
DR EnsemblMetazoa; GMOY003663-RA; GMOY003663-PA; GMOY003663.
DR VEuPathDB; VectorBase:GMOY003663; -.
DR PhylomeDB; A0A1B0FIM4; -.
DR UniPathway; UPA00878; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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:0003735; F:structural constituent of ribosome; IEA:InterPro.
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 GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd09599; M1_LTA4H; 1.
DR CDD; cd00392; Ribosomal_L13; 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; 3.90.1180.10; Ribosomal protein L13; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 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 InterPro; IPR005822; Ribosomal_uL13.
DR InterPro; IPR036899; Ribosomal_uL13_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 Pfam; PF00572; Ribosomal_L13; 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.
DR SUPFAM; SSF52161; Ribosomal protein L13; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361141};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361141};
KW Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751,
KW ECO:0000256|RuleBase:RU361141};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
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 Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR612777-3}.
FT DOMAIN 659..805
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT ACT_SITE 577
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-1"
FT BINDING 334..336
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 459..464
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-3"
FT BINDING 761..763
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR612777-2"
SQ SEQUENCE 808 AA; 92172 MW; 98B6EF8C7917C67C CRC64;
MSICKRVQQW ATFARTWHIY DCTWQNPFDS AKIISKHLMG MNKPIYHPMN DCGDHVVAIN
TKEIALPGDE WIKRVYFHHT GYPGGASWTL AWELHEKDPT MVMKKAVYRS MKGNLQRRYT
MQRLHLYADD KVPEDILANV SHQIKPLRQV PQLLLTFFVV VNCLLFSSRA SRVNLYAKRS
LLKTVPLYLT QKRNIMGRLG KVDPSSYSQP ESITTLHSAL RWQVDFKNTK LVGSVTHKFN
VLEKNLAAII LDVRDIKITN AELICDKSHI PLNHFISESI DDIGAKLTLE LPQGTAPGNL
LVRIDYETSS AASGLQWLTP EQTLGKTHPY MFSQCQAIHA RSILPCQDTP AVKFTYEATV
EHPSDLTALM GALIDKRGPG CTTFKQEVPI PAYLLAIAIG KLVSKPLGPQ SNVWAEQGII
DECAEEFSQT SEMLKTASDI CGPYVWKQYD LLVMPPSFPF GGMENPCLTF VTPTLLAGDK
SLADVVAHEI AHSWTGNLVT NKNFEHFWLN EGFTVFVETK IVGRMHGDKE RDFHMLRNLT
DLQECIRTQL AKQPELTKLV VDLSNCGPDD AFSTVPYIKG STFLRYIEDL LGGPEIFEPF
LRQYLQKYAY KSVITDDFKQ ALYEYFNGTD KKGKLTEIDW DMWLSCEGMP PIIPKFDETL
ANVSKQLAQL WGTKTTSELR DLPDVKQRIS SHQLIDFLGK LIECKGIKDL NEQKIELLET
AYNLKNTKNA EVRFRLMRLY IMARLLDRLD EIIAFANSNF RMKFCRPIYR DLGNWPDARP
KAIENFKRVK DQMMAVCSHT IEKDLGLK
//
