Reviewed,
UniProtKB/Swiss-Prot Q10740 (LKHA4_YEAST)
Last modified
November 25, 2008.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Leukotriene A-4 hydrolase EC=3.3.2.6 Alternative name(s): Leukotriene A(4) hydrolase Short name=LTA-4 hydrolase | ||||
| Gene names |
| ||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4932 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 671 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Hydrolyzes an epoxide moiety of LTA(4) to form LTB(4). The enzyme also has aminopeptidase activity. |
| Catalytic activity | (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Enzyme regulation | Inhibited 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The amiminopeptidase activity is stimulated by LTA(4). |
| Pathway | |
| Subcellular location | |
| Miscellaneous | Present with 5590 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the peptidase M1 family. |
| Biophysicochemical properties | Kinetic parameters: KM=1.5 mM for Leu-p-nitroanilide KM=1.8 mM for Met-p-nitroanilide KM=2.0 mM for Ala-p-nitroanilide Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate pH dependence: Optimum pH is about 7.3. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PRP40 | P33203 | 1 | EBI-10175,EBI-701 | |
| RSP5 | P39940 | 1 | EBI-10175,EBI-16219 | |
| SSM4 | P40318 | 1 | EBI-10175,EBI-18208 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 671 | 671 | Leukotriene A-4 hydrolase | PRO_0000095129 | |||||
Sites | |||||||||
| Active site | 341 | 1 | |||||||
| Active site | 429 | 1 | Proton donor | ||||||
| Metal binding | 340 | 1 | Zinc; catalytic | ||||||
| Metal binding | 344 | 1 | Zinc; catalytic | ||||||
| Metal binding | 363 | 1 | Zinc; catalytic | ||||||
| Site | 244 | 1 | Transition state stabilizer | ||||||
Amino acid modifications | |||||||||
| Modified residue | 51 | 1 | Phosphoserine | ||||||
Experimental info | |||||||||
| Mutagenesis | 244 | 1 | Y → F: Reduces strongly the substrate affinity | ||||||
| Mutagenesis | 316 | 1 | E → A, Q or D: Abolishes the aminopeptidase activity | ||||||
| Mutagenesis | 340 | 1 | H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities | ||||||
| Mutagenesis | 341 | 1 | E → Q: Abolishes the epoxide hydrolase and aminopeptidase activities | ||||||
| Mutagenesis | 344 | 1 | H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities | ||||||
| Mutagenesis | 363 | 1 | E → Q: Abolishes the epoxide hydrolase activity | ||||||
| Mutagenesis | 424 | 1 | F → Y: Increases the epoxide hydrolase activity and decreases the aminopeptidase activity | ||||||
| Mutagenesis | 429 | 1 | Y → F: Abolishes the epoxide hydrolase activity and decreases the aminopeptidase activity | ||||||
| Mutagenesis | 627 | 1 | R → K or A: Abolishes the aminopeptidase activity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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." Nasr F., Becam A.-M., Herbert C.J. Yeast 12:493-499(1996) [PubMed: 8740423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." 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. Hani J.Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | "Cloning and characterization of a bifunctional leukotriene A(4) hydrolase from Saccharomyces cerevisiae." Kull F., Ohlson E., Haeggstroem J.Z. J. Biol. Chem. 274:34683-34690(1999) [PubMed: 10574934] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. |
| [4] | "Saccharomyces cerevisiae leukotriene A4 hydrolase: formation of leukotriene B4 and identification of catalytic residues." Kull F., Ohlson E., Lind B., Haeggstroem J.Z. Biochemistry 40:12695-12703(2001) [PubMed: 11601994] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-340; GLU-341; HIS-344; GLU-363; PHE-424 AND TYR-429. |
| [5] | "Crystallization and X-ray diffraction data analysis of leukotriene A4 hydrolase from Saccharomyces cerevisiae." Andersson B., Kull F., Haeggstroem J.Z., Thunnissen M.M.G.M. Acta Crystallogr. D 59:1093-1095(2003) [PubMed: 12777785] [Abstract] Cited for: CRYSTALLIZATION. |
| [6] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [7] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [8] | "Leukotriene A4 hydrolase, insights into the molecular evolution by homology modeling and mutational analysis of enzyme from Saccharomyces cerevisiae." Tholander F., Kull F., Ohlson E., Shafqat J., Thunnissen M.M.G.M., Haeggstroem J.Z. J. Biol. Chem. 280:33477-33486(2005) [PubMed: 16024909] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS. |
| [9] | "A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A4 hydrolase stabilizes the transition state of the peptidase activity." Thompson M.W., Archer E.D., Romer C.E., Seipelt R.L. Peptides 27:1701-1709(2006) [PubMed: 16597475] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-244. |
| [10] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X94547 Genomic DNA. Translation: CAA64237.1. Z71321 Genomic DNA. Translation: CAA95912.1. | |
| PIR | S61099. |
| RefSeq | NP_014353.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HS6 based on UniProtKB P09960. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:4371N. |
| IntAct | Q10740. |
Proteomic databases | |
| PeptideAtlas | Q10740. |
Genome annotation databases | |
| Ensembl | YNL045W. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 855682. |
| GenomeReviews | Gene locus YNL045W in contig Y13139_GR. |
| KEGG | sce:YNL045W. |
| NMPDR | fig|4932.3.peg.5429. |
Organism-specific databases | |
| CYGD | YNL045w. |
| SGD | S000004990. YNL045W. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | Q10740. |
Gene expression databases | |
| GermOnline | YNL045W. Saccharomyces cerevisiae. |
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] |
| PANTHER | PTHR11533. Peptidase_M1. 1 hit. |
| Pfam | PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view] |
| PRINTS | PR00756. ALADIPTASE. |
| TIGRFAMs | TIGR02411. leuko_A4_hydro. 1 hit. |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| LinkHub | Q10740. |
| NextBio | 979984. |
Entry information
| Entry name | LKHA4_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q10740 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XIV Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names |

Clusters with


