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Database: UniProt
Entry: LKHA4_CHAGB
LinkDB: LKHA4_CHAGB
Original site: LKHA4_CHAGB 
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   20-JUN-2018, entry version 68.
DE   RecName: Full=Leucine aminopeptidase 2;
DE            EC=3.4.11.-;
DE   AltName: Full=Epoxide hydrolase;
DE            EC=3.3.2.10;
DE   AltName: Full=Leukotriene A-4 hydrolase homolog;
DE            Short=LTA-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;
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium
RT   globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Aminopeptidase that preferentially cleaves di- and
CC       tripeptides. Also has low epoxide hydrolase activity (in vitro).
CC       Can hydrolyze the epoxide leukotriene LTA(4) but it forms
CC       preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid
CC       rather than the cytokine leukotriene B(4) as the product compared
CC       to the homologous mammalian enzyme (in vitro).
CC       {ECO:0000250|UniProtKB:Q10740}.
CC   -!- CATALYTIC ACTIVITY: An epoxide + H(2)O = a glycol.
CC       {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}.
CC       Nucleus {ECO:0000250|UniProtKB:Q10740}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
DR   EMBL; CH408033; EAQ85880.1; -; Genomic_DNA.
DR   RefSeq; XP_001224789.1; XM_001224788.1.
DR   ProteinModelPortal; Q2GY21; -.
DR   SMR; Q2GY21; -.
DR   STRING; 306901.XP_001224789.1; -.
DR   MEROPS; M01.034; -.
DR   EnsemblFungi; EAQ85880; EAQ85880; CHGG_07133.
DR   GeneID; 4393714; -.
DR   eggNOG; KOG1047; Eukaryota.
DR   eggNOG; COG0308; LUCA.
DR   InParanoid; Q2GY21; -.
DR   OrthoDB; EOG092C0ZZE; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0005771; C:multivesicular body; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0061957; C:NVT complex; IEA:EnsemblFungi.
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:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR   GO; GO:0030163; P:protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0120113; P:protein localization by the NVT pathway; IEA:EnsemblFungi.
DR   CDD; cd09599; M1_LTA4H; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 1.25.40.320; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012777; Leukotriene_A4_hydrolase.
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_N.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PTHR11533; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
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; Metal-binding;
KW   Metalloprotease; Nucleus; Protease; Reference proteome; Zinc.
FT   CHAIN         1    611       Leucine aminopeptidase 2.
FT                                /FTId=PRO_0000324926.
FT   REGION      135    137       Substrate binding. {ECO:0000250}.
FT   REGION      265    270       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    295    295       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   ACT_SITE    383    383       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       294    294       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       298    298       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       317    317       Zinc; catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
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
//
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