Type of Issue: Erroneous source or erroneous propagation, or other issue
propagation
https://www.pombase.org/reference/PMID:27558664
Cys2 is a serine O-acetyltransferase required for
cysteine biosynthesis
Functional profiling revealed that Cys2 is essential for As/Cd tolerance
(Table S5). Cys2 has greatest sequence homology to homoserine
O-acetyltransferases, predicting that it should be involved with
methionine biosynthesis. However, as noted previously, Met6 is also
predicted to be a homoserine O-acetyltransferase (Ma et al. 2007).
S. cerevisiae homoserine O-acetyltransferase Met2 is significantly more
similar to Met6 than Cys2 in S. pombe, suggesting that in S. pombe Met6
is more likely the authentic homoserine O-acetyltransferase (Figure 3).
Furthermore, met6D mutants require methionine supplementation
for growth on defined minimal medium whereas cys2D cells require
cysteine supplementation (Ma et al. 2007). Thus our data showing that
cys2D but not met6D cells are highly sensitive to As/Cd toxicity, as well
as our data indicating that methionine biosynthesis is not required for
cadmium or arsenic resistance, support the notion that Cys2 is actually
a serine O-acetyltransferase that is specifically essential for cysteine
biosynthesis (Figure 3).
(I'll add a NOT annotation for this one)
Add the label 'high priority' if needed. Generally high priority issues affect a lot of proteins, and annotations are incorrect (as opposed to just imprecise).
GO:0004414 | homoserine O-acetyltransferase activity | IBA with S000005221 , PTN000791315 , Q8F4I0 , CAL0000174790 , met6 , P45131
https://www.pombase.org/gene/SPBC106.17c
propagation
https://www.pombase.org/reference/PMID:27558664 Cys2 is a serine O-acetyltransferase required for cysteine biosynthesis Functional profiling revealed that Cys2 is essential for As/Cd tolerance (Table S5). Cys2 has greatest sequence homology to homoserine O-acetyltransferases, predicting that it should be involved with methionine biosynthesis. However, as noted previously, Met6 is also predicted to be a homoserine O-acetyltransferase (Ma et al. 2007). S. cerevisiae homoserine O-acetyltransferase Met2 is significantly more similar to Met6 than Cys2 in S. pombe, suggesting that in S. pombe Met6 is more likely the authentic homoserine O-acetyltransferase (Figure 3). Furthermore, met6D mutants require methionine supplementation for growth on defined minimal medium whereas cys2D cells require cysteine supplementation (Ma et al. 2007). Thus our data showing that cys2D but not met6D cells are highly sensitive to As/Cd toxicity, as well as our data indicating that methionine biosynthesis is not required for cadmium or arsenic resistance, support the notion that Cys2 is actually a serine O-acetyltransferase that is specifically essential for cysteine biosynthesis (Figure 3).
(I'll add a NOT annotation for this one)