LKHA4_BOTFB
ID LKHA4_BOTFB Reviewed; 616 AA.
AC A6SAG8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Leukotriene A-4 hydrolase homolog;
DE Short=LTA-4 hydrolase;
DE EC=3.3.2.6;
DE AltName: Full=Leukotriene A(4) hydrolase;
GN ORFNames=BC1G_09514;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Aminopeptidase that preferentially cleaves tripeptides. Also
CC has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide
CC moiety of LTA(4) to form LTB(4) (in vitro) (By similarity).
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN30453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH476904; EDN30453.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001551808.1; XM_001551758.1.
DR AlphaFoldDB; A6SAG8; -.
DR SMR; A6SAG8; -.
DR MEROPS; M01.034; -.
DR World-2DPAGE; 0005:A6SAG8; -.
DR GeneID; 5432324; -.
DR KEGG; bfu:BCIN_09g05630; -.
DR UniPathway; UPA00878; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004301; F:epoxide hydrolase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 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 PANTHER; PTHR45726; PTHR45726; 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; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
DR TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Leukotriene biosynthesis; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Zinc.
FT CHAIN 1..616
FT /note="Leukotriene A-4 hydrolase homolog"
FT /id="PRO_0000324923"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 394
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277..282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 616 AA; 69504 MW; 08A0FB6C96FAC325 CRC64;
MATVSTINMP RDPNTLSNYN NWRTKHTIAD LAIDFTKQRV HGTVTLQLES ITDKESEEII
LDTSFVDVQS VAVDGNKTGE WTLEKRIEPF GTPLSVKIPG GAAKGTVIAL AITLSTTDKC
TALQWLTPAQ TSNKKFPYMF SQCQAIHNRS IFPCQDTPDV KSTYDFRIRS PLPVLASGLP
RGAGSFVHGE NGESGTLLYS FYQEIPMPSY LFALASGDIA TASIGPRSLV STGPEELIGA
KWELERDTEK FIETIEKIVY PYEWTQYNVL VLPPSFPYGG MENPVFTFAT PTIISGDREN
VDVVAHELAH SWSGNLVSNA SWEHFWLNEG WTVYLERRII AAVHGEAYRD FSSIIGWKAL
EDSVKLYGED HEFTKLIVDL KGKDPDDAFS SVPYEKGFHF LYYLERLVGK PSWDKFIPHY
FTTWKKKSLD SYDFKATLLD FFASDSAASK ALESVDWDSW FYKPGLPSKP EFDTSLVDKC
YALAKKWESK DYTPSPSDIE GWAANQVVVF LQQVQLFTTP LTPVQSQAMG KAYNLVNTKN
VELSSRYFGV GLAAKDETVY QPTAELLGKV GRMKFVRTLY RKLVVVDRKL AVETFEKNKD
FYHPICRDQV EKDLKE
