lys2 (SPAC343.16; UniProt Q9UT74), the fission yeast ortholog of S. cerevisiae LYS4, encodes mitochondrial homoaconitase (EC 4.2.1.36), a [4Fe-4S] aconitase-family hydratase. It hydrates cis-homoaconitate to homoisocitrate in the alpha-aminoadipate pathway of lysine biosynthesis. The cloned gene complements the classical lys2-97 auxotroph and is used as a selectable marker. It is mitochondrial in a genome-wide screen.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004409 homoaconitate hydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC/RHEA and InterPro mapping of homoaconitase. Supporting Evidence: PMID:16491385 we used genetic mapping data and genomic sequence information to predict the identity of the S. pombe lys2(+) gene, which is homologous to Saccharomyces cerevisiae LYS4(+) |
| GO:0004409 homoaconitate hydratase activity | ISO PMID:16491385 Cloning the Schizosaccharomyces pombe lys2+ gene and constru... | ACCEPT | Summary: lys2 is the S. cerevisiae LYS4 (homoaconitase) homolog and complements the lys2-97 auxotroph. Supporting Evidence: PMID:16491385 We confirmed this prediction, showing that the cloned SPAC343.16 gene can complement a lys2-97 mutant allele PMID:16491385 we used genetic mapping data and genomic sequence information to predict the identity of the S. pombe lys2(+) gene, which is homologous to Saccharomyces cerevisiae LYS4(+) |
| GO:0005739 mitochondrion | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome screen: mitochondrion, as for S. cerevisiae Lys4. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping (mitochondrion), derived from the localisation screen. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005759 mitochondrial matrix | IMP PMID:16491385 Cloning the Schizosaccharomyces pombe lys2+ gene and constru... | ACCEPT | Summary: Matrix location by orthology to S. cerevisiae LYS4 (the curator read the full text). Supporting Evidence: PMID:16491385 we used genetic mapping data and genomic sequence information to predict the identity of the S. pombe lys2(+) gene, which is homologous to Saccharomyces cerevisiae LYS4(+) |
| GO:0009085 L-lysine biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro mapping; consistent. Supporting Evidence: PMID:16491385 We confirmed this prediction, showing that the cloned SPAC343.16 gene can complement a lys2-97 mutant allele |
| GO:0009085 L-lysine biosynthetic process | IMP PMID:16491385 Cloning the Schizosaccharomyces pombe lys2+ gene and constru... | ACCEPT | Summary: lys2 complements the lys2-97 lysine auxotroph. Supporting Evidence: PMID:16491385 We confirmed this prediction, showing that the cloned SPAC343.16 gene can complement a lys2-97 mutant allele |
| GO:0009085 L-lysine biosynthetic process | IMP PMID:17622533 Six new amino acid-auxotrophic markers for targeted gene int... | ACCEPT | Summary: Auxotrophic marker screen. Supporting Evidence: PMID:17622533 Mutants that were auxotrophic for arginine, asparagine, cysteine, lysine, methionine and phenylalanine were isolated. |
| GO:0009085 L-lysine biosynthetic process | IMP PMID:3142867 Lysine biosynthesis pathway and biochemical blocks of lysine... | ACCEPT | Summary: Classical lysine auxotroph (lys2-97) blocked before aminoadipate. Supporting Evidence: PMID:3142867 Of the eight enzyme activities of the AA pathway that have been examined so far, six were present in the extract of wild-type S. pombe cells. |
| GO:0051539 4 iron, 4 sulfur cluster binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Aconitase-family [4Fe-4S] cluster binding; subsidiary. Supporting Evidence: PMID:16491385 we used genetic mapping data and genomic sequence information to predict the identity of the S. pombe lys2(+) gene, which is homologous to Saccharomyces cerevisiae LYS4(+) |
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)