LKA41_PICST
ID LKA41_PICST Reviewed; 626 AA.
AC A3LRX6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Leucine aminopeptidase 2-1;
DE EC=3.4.11.-;
DE AltName: Full=Epoxide hydrolase;
DE EC=3.3.2.10;
DE AltName: Full=Leukotriene A-4 hydrolase homolog 1;
DE Short=LTA-4 hydrolase 1;
GN Name=LKA4; ORFNames=PICST_76777;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- FUNCTION: Aminopeptidase that preferentially cleaves di- and
CC tripeptides. Also has low epoxide hydrolase activity (in vitro). Can
CC hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially
CC 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine
CC leukotriene B(4) as the product compared to the homologous mammalian
CC enzyme (in vitro). {ECO:0000250|UniProtKB:Q10740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594;
CC EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:Q10740};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q10740};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q10740};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10740}. Nucleus
CC {ECO:0000250|UniProtKB:Q10740}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; CP000497; ABN65808.2; -; Genomic_DNA.
DR RefSeq; XP_001383837.2; XM_001383800.1.
DR AlphaFoldDB; A3LRX6; -.
DR SMR; A3LRX6; -.
DR STRING; 4924.XP_001383837.2; -.
DR MEROPS; M01.034; -.
DR EnsemblFungi; ABN65808; ABN65808; PICST_76777.
DR GeneID; 4837771; -.
DR KEGG; pic:PICST_76777; -.
DR eggNOG; KOG1047; Eukaryota.
DR HOGENOM; CLU_014505_1_2_1; -.
DR InParanoid; A3LRX6; -.
DR OMA; ELRFRWY; -.
DR OrthoDB; 775595at2759; -.
DR Proteomes; UP000002258; Chromosome 3.
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: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; Metal-binding; Metalloprotease; Nucleus; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..626
FT /note="Leucine aminopeptidase 2-1"
FT /id="PRO_0000324938"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 389
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 134..136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259..264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 626 AA; 71543 MW; FD6212CA990E2688 CRC64;
MSKFENISKR SHELDPCTNS NYAEFKVVHT DLSLSVSFES KNISGNVIYT LKKLTKTNRL
VLDTSFLEVS TAKVNGKEVV FELLPHKAPF GSPLVIPIDG ENESLTVEVD FRTTDKCTAI
QFIQGDTGPY VFSQCQAIHA RSLFPCFDTP GVKSPYKFTA KSPSVCTMSG RPQPSNEAGV
YHFDQPIPIP SYLVSITSGN LHKAPIGPRS DVYSEEPSLK DCQWEFEKDM ENFIQIAEKI
VFEYEWSRFD SLVLPSSFPY GGMEIPNMTQ LTPTLISKDR TQVKVMAHEL AHSWSGNLVT
NCSWEHFWLN EGWTVYLERR IIGAIAAAEA QEEGRANPEK YGEQVRHFNA IIGWNALVET
VESFDPKFTS LVWDLASGDP DDAFSRIPYE KGFNFLFHIE TKVGGTKEFD PFIKHYFKKF
RYQSLNSAQF IETLYDFYTP LGKKDALDTI DLEKWLFQPG LPDDPKFDTT LADQVYVLVE
KWVDFVKSGE TEVKFSEADV KEFEGEQEML FIETLTDRFK DLDVSPELIR KLPSIYPKYA
ASKNGEVLAR WNELLIKYGN YTSSDEQVKF FADWLGTVGR MKYVRPGYKL LQTSVSIEFA
VETFKRFEDK YHPICKTMVQ KDLNLA
