ID LKHA4_CHAGB Reviewed; 611 AA.
AC Q2GY21;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 44.
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=CHGG_07133;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC
OS 6347 / NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Kodira C.D.,
RA Yandava C., Zeng Q., Alvarado L., Oleary S., Untereiner W.;
RT "Annotation of the Chaetomium globosum CBS 148.51 genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408033; EAQ85880.1; -; Genomic_DNA.
DR RefSeq; XP_001224789.1; XM_001224788.1.
DR ProteinModelPortal; Q2GY21; -.
DR MEROPS; M01.034; -.
DR GeneID; 4393714; -.
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 1 611 Leukotriene A-4 hydrolase homolog.
FT /FTId=PRO_0000324926.
FT REGION 135 137 Substrate binding (By similarity).
FT REGION 265 270 Substrate binding (By similarity).
FT ACT_SITE 295 295 Proton acceptor (By similarity).
FT ACT_SITE 383 383 Proton donor (By similarity).
FT METAL 294 294 Zinc; catalytic (By similarity).
FT METAL 298 298 Zinc; catalytic (By similarity).
FT METAL 317 317 Zinc; catalytic (By similarity).
SQ SEQUENCE 611 AA; 69072 MW; DCF0315477CB52A3 CRC64;
MAPVRDPNTL SNYNEWRTKH TTADFKVDFT AKCLRGSVVL ELESQTDKAS KEIILDSSYV
DVSAITLNST PSQWEVRDRT GPSGSPVRVA VPNGAGKGEV VKLEIELATT DKCTALQWLT
PAQTSNKKAP FMFSQCQAIH ARSIFPCQDT PDVKSTYDFI IRSPHVVVAS GVPVPGEPES
VGEDKVYKFH QKVPIPSYLF AVASGDIASA KIGRCSSVAT GPNELKASQW ELEDDMDKFL
DAAEKIVFPY QWGEYNVLVL PPSFPYGGME NPIFTFATPT IISGDRQNID VIAHELAHSW
SGNLVTSCSW EHFWLNEGWT VYLERRILAS IHKNDSYFDF SAIIGWKHLE EAIEEFGKDH
EYTKLSIKHD GIDPDDAFSS VPYEKGFHFI WSLDRLVGRE NFDKFIPHYF SKWQNKSLDS
FEFKDTFLEF FSAPEYSKLK DKISQIDWEG RFFNPGLPPK PEFDTTLVDG CFQLANKWKS
KDFSPSPSDT SSWTGNQLLV FLNVVQDFEE PLTAEQSQNM GKIYALADSK NVELKAAYYQ
IAMKAKDTTS YPGVAELLGN VGRMKFVRTL FRTLNKVDRD LAVKTFQKNR DFYHPICRQL
VEKDLGLGES K
//
