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UniProtKB/Swiss-Prot entry Q10740


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LKHA4_YEAST
Primary accession number Q10740
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 82)
Name and origin of the protein
Protein name Leukotriene A-4 hydrolase
Synonyms EC 3.3.2.6
Leukotriene A(4) hydrolase
LTA-4 hydrolase
Gene name
OrderedLocusNames: YNL045W
ORFNames: N2535
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(199604)12:5<493::AID-YEA929>3.3.CO;2-N; PubMed=8740423 [NCBI, ExPASy, EBI, Israel, Japan]
Nasr F., Becam A.-M., Herbert C.J.;
"The sequence of 12.8 kb from the left arm of chromosome XIV reveals a sigma element, a pro-tRNA and six complete open reading frames, one of which encodes a protein similar to the human leukotriene A4 hydrolase.";
Yeast 12:493-499(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
DOI=10.1074/jbc.274.49.34683; PubMed=10574934 [NCBI, ExPASy, EBI, Israel, Japan]
Kull F., Ohlson E., Haeggstroem J.Z.;
"Cloning and characterization of a bifunctional leukotriene A(4) hydrolase from Saccharomyces cerevisiae.";
J. Biol. Chem. 274:34683-34690(1999).
[4]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-340; GLU-341; HIS-344; GLU-363; PHE-424 AND TYR-429.
DOI=10.1021/bi011348p; PubMed=11601994 [NCBI, ExPASy, EBI, Israel, Japan]
Kull F., Ohlson E., Lind B., Haeggstroem J.Z.;
"Saccharomyces cerevisiae leukotriene A4 hydrolase: formation of leukotriene B4 and identification of catalytic residues.";
Biochemistry 40:12695-12703(2001).
[5]
CRYSTALLIZATION.
DOI=10.1107/S0907444903007728; PubMed=12777785 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson B., Kull F., Haeggstroem J.Z., Thunnissen M.M.G.M.;
"Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae.";
Acta Crystallogr. D 59:1093-1095(2003).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS.
DOI=10.1074/jbc.M506821200; PubMed=16024909 [NCBI, ExPASy, EBI, Israel, Japan]
Tholander F., Kull F., Ohlson E., Shafqat J., Thunnissen M.M.G.M., Haeggstroem J.Z.;
"Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae.";
J. Biol. Chem. 280:33477-33486(2005).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-244.
DOI=10.1016/j.peptides.2006.02.006; PubMed=16597475 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson M.W., Archer E.D., Romer C.E., Seipelt R.L.;
"A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A4 hydrolase stabilizes the transition state of the peptidase activity.";
Peptides 27:1701-1709(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X94547; CAA64237.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71321; CAA95912.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61099; S61099.
RefSeq NP_014353.1; -.
3D structure databases
HSSP P09960; 1HS6. [HSSP ENTRY / PDB]
ModBase Q10740.
Protein-protein interaction databases
DIP DIP:4371N; -.
IntAct Q10740; -.
Organism-specific databases
CYGD YNL045w; -.
SGD S000004990; YNL045W.
Yeast-GFP YNL045W.
Gene expression databases
GermOnline YNL045W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0004177; Molecular function: aminopeptidase activity (inferred from direct assay from SGD).
GO:0004301; Molecular function: epoxide hydrolase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006629; Biological process: lipid metabolic process (inferred from direct assay from SGD).
GO:0030163; Biological process: protein catabolic process (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR012777; Leuk_A4_hydro_aminopept.
IPR006025; Pept_M_Zn_BS.
IPR001930; Peptidase_M1.
IPR015211; Peptidase_M1_C.
IPR014782; Peptidase_M1_N.
Graphical view of domain structure.
PANTHER PTHR11533; Peptidase_M1; 1.
Pfam PF09127; Leuk-A4-hydro_C; 1.
PF01433; Peptidase_M1; 1.
Pfam graphical view of domain structure.
PRINTS PR00756; ALADIPTASE.
TIGRFAMs TIGR02411; leuko_A4_hydro; 1.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS Q10740.
Proteomic databases
PeptideAtlas Q10740; -.
Genome annotation databases
Ensembl YNL045W; Saccharomyces cerevisiae. [Contig view]
GeneID 855682; -.
GenomeReviews Y13139_GR; YNL045W.
KEGG sce:YNL045W; -.
NMPDR fig|4932.3.peg.5429; -.
Phylogenomic databases
HOGENOM Q10740; -.
Other
LinkHub Q10740; -.
ProtoNet Q10740.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Hydrolase; Leukotriene biosynthesis; Metal-binding; Metalloprotease; Multifunctional enzyme; Nucleus; Phosphoprotein; Protease; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   671  671     Leukotriene A-4 hydrolase. PRO_0000095129
ACT_SITE   341   341         
ACT_SITE   429   429        Proton donor. 
METAL   340   340        Zinc; catalytic. 
METAL   344   344        Zinc; catalytic. 
METAL   363   363        Zinc; catalytic. 
SITE   244   244  1     Transition state stabilizer. 
MOD_RES   51    51        Phosphoserine. 
MUTAGEN   244   244        Y->F: Reduces strongly the substrate affinity. 
MUTAGEN   316   316        E->A,Q,D: Abolishes the aminopeptidase activity. 
MUTAGEN   340   340        H->Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 
MUTAGEN   341   341        E->Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 
MUTAGEN   344   344        H->Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 
MUTAGEN   363   363        E->Q: Abolishes the epoxide hydrolase activity. 
MUTAGEN   424   424        F->Y: Increases the epoxide hydrolase activity and decreases the aminopeptidase activity. 
MUTAGEN   429   429        Y->F: Abolishes the epoxide hydrolase activity and decreases the aminopeptidase activity. 
MUTAGEN   627   627        R->K,A: Abolishes the aminopeptidase activity. 
Sequence information
Length: 671 AA [This is the length of the unprocessed precursor] Molecular weight: 77353 Da [This is the MW of the unprocessed precursor] CRC64: 454E40F030BF28FA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP SRSPEYDQST 

        70         80         90        100        110        120 
LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK NKSDELHLDT SYLDVQEVHI 

       130        140        150        160        170        180 
DGSKADFQIE QRKEPLGSRL VINNASCNDN FTLNIQFRTT DKCTALQWLN SKQTKGGKPY 

       190        200        210        220        230        240 
VFSQLEAIHA RSLFPCFDTP SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP 

       250        260        270        280        290        300 
IPAYLIGIAS GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT 

       310        320        330        340        350        360 
YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL VTNCSWNHFW 

       370        380        390        400        410        420 
LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS MKDPERFSTL VQNLNDNTDP 

       430        440        450        460        470        480 
DDAFSTVPYE KGFNLLFHLE TILGGKAEFD PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE 

       490        500        510        520        530        540 
KKEILDSVDW ETWLYKPGMP PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI 

       550        560        570        580        590        600 
DIKDFNSNQL VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF 

       610        620        630        640        650        660 
KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF DKFKDTYHPI 

       670 
CKALVKQDLG L 

Q10740 in FASTA format

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