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 01-MAY-2013, entry version 45.
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).
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: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
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DR EMBL; CH408159; EDK40349.2; -; Genomic_DNA.
DR RefSeq; XP_001483718.1; XM_001483668.1.
DR ProteinModelPortal; A5DME6; -.
DR GeneID; 5125528; -.
DR KEGG; pgu:PGUG_04447; -.
DR eggNOG; COG0308; -.
DR KO; K01254; -.
DR OrthoDB; EOG49KJZX; -.
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: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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; ARM-type_fold; 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; Zinc.
FT CHAIN 1 615 Leukotriene A-4 hydrolase homolog 1.
FT /FTId=PRO_0000324936.
FT REGION 137 139 Substrate binding (By similarity).
FT REGION 261 266 Substrate binding (By similarity).
FT ACT_SITE 291 291 Proton acceptor (By similarity).
FT ACT_SITE 380 380 Proton donor (By similarity).
FT METAL 290 290 Zinc; catalytic (By similarity).
FT METAL 294 294 Zinc; catalytic (By similarity).
FT METAL 313 313 Zinc; catalytic (By similarity).
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
//
