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Database: UniProt
Entry: LKA41_PICGU
LinkDB: LKA41_PICGU
Original site: LKA41_PICGU 
ID   LKA41_PICGU             Reviewed;         615 AA.
AC   A5DME6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   26-NOV-2014, entry version 52.
DE   RecName: Full=Leukotriene A-4 hydrolase homolog 1;
DE            Short=LTA-4 hydrolase 1;
DE            EC=3.3.2.6;
DE   AltName: Full=Leukotriene A(4) hydrolase;
GN   ORFNames=PGUG_04447;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM
OS   1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
RA   Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
RA   Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
RA   Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
RA   Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
RA   Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
RA   Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Aminopeptidase that preferentially cleaves tripeptides.
CC       Also has low epoxide hydrolase activity (in vitro). Can hydrolyze
CC       an epoxide moiety of LTA(4) to form LTB(4) (in vitro) (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-
CC       7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-
CC       dihydroxyicosa-6,8,10,14-tetraenoate.
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
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; CH408159; EDK40349.2; -; Genomic_DNA.
DR   RefSeq; XP_001483718.1; XM_001483668.1.
DR   ProteinModelPortal; A5DME6; -.
DR   STRING; 4929.A5DME6; -.
DR   MEROPS; M01.034; -.
DR   GeneID; 5125528; -.
DR   KEGG; pgu:PGUG_04447; -.
DR   eggNOG; COG0308; -.
DR   InParanoid; A5DME6; -.
DR   KO; K01254; -.
DR   OrthoDB; EOG7DFXMZ; -.
DR   UniPathway; UPA00878; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012777; Leukotriene_A4_hydrolase.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_N.
DR   PANTHER; PTHR11533; PTHR11533; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Leukotriene biosynthesis;
KW   Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN         1    615       Leukotriene A-4 hydrolase homolog 1.
FT                                /FTId=PRO_0000324936.
FT   REGION      137    139       Substrate binding. {ECO:0000250}.
FT   REGION      261    266       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    291    291       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   ACT_SITE    380    380       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       290    290       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       294    294       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       313    313       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
SQ   SEQUENCE   615 AA;  70392 MW;  B41C65A30CC891C7 CRC64;
     MLRRPKVSPE LDPSTLSNYG DFIVHKTQLD LAVDFDKNRV SSCVSLNVTN RTNTHQVVLD
     SSYLVIHSAS INGISTPFDV AERQTLGSKV TIKIPPEMKI SELTITIESE TTYECTALQF
     LPAEATDGGV GPYLFSQCQA IHARSLFPCF DTPAVKCPYE MSVTSPYPSV MSGRPLGVSG
     NMYRFSQPVP IPSYLVAVAS GDIKSAPIGP RSSVYCEPLK LEVCQHEFQA DMEHFLQAAE
     SLVFKYEWER YDALVLPSSF PYGGMENPNI TFVTPTLISG DRENVDVIAH ELAHSWSGNL
     VTNCSWEHFW LNEGWTVYLE RRILGKLHGN ATRDFSAIIG WTDLENSIAA MGPSAERWSM
     LVHNLKDGSD PDDAFSTVPY EKGSTLLYHI ETLIGQEKFD KFIPHYFHTF RYKSLDTYQF
     IDCLYSFFAD FKSVLDTIDW ESWLYKPGMP PVKPDFDTSM VDQCYQLADK WYHHSLKNKF
     HKFSSEDIKS FTANQSVVFL DTLIAFDKLD FKWKHHLDAL NTMASVYQEY SKSTNAEVLF
     RWYVLQVTGH NQEYYSRLGE WLGTVGRMKF VRPGYVLLNK VDRSMALHYF EKFHNRYHAI
     CKSMVRRDWD LIKTK
//
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