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LACCA:DYR
Contents
Species (Taxon ID) | Lactobacillus casei. (1582) | |
Gene Name(s) | folA (synonyms: dhfR) | |
Protein Name(s) | Dihydrofolate reductase | |
External Links | ||
UniProt | P00381 | |
EMBL | M10922 | |
PIR | A24036 | |
PDB | 1AO8 1BZF 1DIS 1DIU 1LUD 2HM9 2HQP 2L28 2LF1 3DFR | |
PDBsum | 1AO8 1BZF 1DIS 1DIU 1LUD 2HM9 2HQP 2L28 2LF1 3DFR | |
ProteinModelPortal | P00381 | |
SMR | P00381 | |
BindingDB | P00381 | |
ChEMBL | CHEMBL2902 | |
BRENDA | 1.5.1.3 | |
SABIO-RK | P00381 | |
UniPathway | UPA00077 | |
EvolutionaryTrace | P00381 | |
GO | GO:0004146 GO:0050661 GO:0006545 GO:0009165 GO:0006730 GO:0046677 GO:0031427 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:0050661 |
NADP binding |
ECO:0000314 |
F |
Using crystallography, scientists determined that when NADPH binds to dihydrofolate reductase, the enzyme:substrate complex geometry stands out. Nicotinamide interacts with 3 oxygen atoms and 3 hydrogen atoms in this very polar environment. |
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:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0031427 |
response to methotrexate |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0046677 |
response to antibiotic |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006730 |
one-carbon metabolic process |
ECO:0000322 |
imported manually 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.
- ↑ Filman, DJ et al. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis. J. Biol. Chem. 257 13663-72 PubMed GONUTS page