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STREE:O85255
Contents
Species (Taxon ID) | Streptococcus pneumoniae. (1313) | |
Gene Name(s) | dfr (ECO:0000313 with EMBL:AAC33861.1) (synonyms: dhfr (ECO:0000313 with EMBL:AAG22523.1)) | |
Protein Name(s) | Dihydrofolate reductase (ECO:0000256 with PIRNR:PIRNR000194) | |
External Links | ||
UniProt | O85255 | |
EMBL | AF055720 AF288414 AF288418 | |
ProteinModelPortal | O85255 | |
UniPathway | UPA00077 | |
GO | GO:0004146 GO:0050661 GO:0006545 GO:0009165 GO:0006730 GO:0046654 | |
Gene3D | 3.40.430.10 | |
InterPro | IPR012259 IPR024072 IPR017925 IPR001796 | |
Pfam | PF00186 | |
PIRSF | PIRSF000194 | |
PRINTS | PR00070 | |
SUPFAM | SSF53597 | |
PROSITE | PS00075 PS51330 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000315 |
F |
Figure 8 shows how the mutation of Val100 to Leu makes the leucine side chain clash with side chains of Ile8 and Phe34, shifting their positions and stacking interactions with the trimethoprim molecule. "Weaker binding of trimethoprim to Leu100 DHFR would lead to trimethoprim resistance". The KM values of NADPH and H2F for the wild type spDHFR and the mutant Sp9 were measured (Table 2B). The KM values for the wild type spDHFR were at least order of magnitude higher than those for the Sp9 mutant that showed full enzyme activity even at a limiting low concentration of 0.63 μM H2F consistent with a much lower KM value for this substrate. |
complete | |||||
enables |
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006545 |
glycine biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0046654 |
tetrahydrofolate biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0050661 |
NADP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006730 |
one-carbon metabolic process |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0046654 |
tetrahydrofolate biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00077 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Lee, J et al. (2010) Kinetic and structural characterization of dihydrofolate reductase from Streptococcus pneumoniae. Biochemistry 49 195-206 PubMed GONUTS page