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ECOLI:DYR
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | folA (synonyms: tmrA) | |
Protein Name(s) | Dihydrofolate reductase | |
External Links | ||
UniProt | P0ABQ4 | |
EMBL | J01609 X05108 U00096 AP009048 | |
PIR | A93704 | |
RefSeq | NP_414590.1 YP_488354.1 | |
PDB | 1DDR 1DDS 1DHI 1DHJ 1DRA 1DRB 1DRE 1DRH 1DYH 1DYI 1DYJ 1JOL 1JOM 1RA1 1RA2 1RA3 1RA8 1RA9 1RB2 1RB3 1RC4 1RD7 1RE7 1RF7 1RG7 1RH3 1RX1 1RX2 1RX3 1RX4 1RX5 1RX6 1RX7 1RX8 1RX9 1TDR 2ANO 2ANQ 2D0K 2DRC 2INQ 3DAU 3DRC 3K74 3KFY 3OCH 3QL3 3QYL 3QYO 3R33 4DFR 4EIG 4EIZ 4EJ1 4FHB 4GH8 4I13 4I1N 4KJJ 4KJK 4KJL 4NX6 4NX7 5DFR 6DFR 7DFR | |
PDBsum | 1DDR 1DDS 1DHI 1DHJ 1DRA 1DRB 1DRE 1DRH 1DYH 1DYI 1DYJ 1JOL 1JOM 1RA1 1RA2 1RA3 1RA8 1RA9 1RB2 1RB3 1RC4 1RD7 1RE7 1RF7 1RG7 1RH3 1RX1 1RX2 1RX3 1RX4 1RX5 1RX6 1RX7 1RX8 1RX9 1TDR 2ANO 2ANQ 2D0K 2DRC 2INQ 3DAU 3DRC 3K74 3KFY 3OCH 3QL3 3QYL 3QYO 3R33 4DFR 4EIG 4EIZ 4EJ1 4FHB 4GH8 4I13 4I1N 4KJJ 4KJK 4KJL 4NX6 4NX7 5DFR 6DFR 7DFR | |
DisProt | DP00301 | |
ProteinModelPortal | P0ABQ4 | |
SMR | P0ABQ4 | |
DIP | DIP-35824N | |
IntAct | P0ABQ4 | |
MINT | MINT-1239602 | |
STRING | 511145.b0048 | |
BindingDB | P0ABQ4 | |
ChEMBL | CHEMBL2364669 | |
SWISS-2DPAGE | P0ABQ4 | |
PaxDb | P0ABQ4 | |
PRIDE | P0ABQ4 | |
EnsemblBacteria | AAC73159 BAB96616 | |
GeneID | 12933205 944790 | |
KEGG | ecj:Y75_p0048 eco:b0048 | |
PATRIC | 32115195 | |
EchoBASE | EB0322 | |
EcoGene | EG10326 | |
eggNOG | COG0262 | |
HOGENOM | HOG000040233 | |
InParanoid | P0ABQ4 | |
KO | K00287 | |
OMA | TSYAFVH | |
OrthoDB | EOG6KT2V2 | |
PhylomeDB | P0ABQ4 | |
BioCyc | EcoCyc:DIHYDROFOLATEREDUCT-MONOMER ECOL316407:JW0047-MONOMER MetaCyc:DIHYDROFOLATEREDUCT-MONOMER | |
SABIO-RK | P0ABQ4 | |
UniPathway | UPA00077 | |
EvolutionaryTrace | P0ABQ4 | |
PRO | PR:P0ABQ4 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P0ABQ4 | |
GO | GO:0004146 GO:0050661 GO:0009257 GO:0046656 GO:0006545 GO:0009165 GO:0006730 GO:0046677 GO:0042493 GO:0031427 | |
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 |
Typically, dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). DHFR acts in a catalytic cycle of 5 different intermediates. In the mutant (by changing Leu 28 to Phe), the dissociation rate of the enzyme:substrate complex increases by 10-20 fold. In addition, the rates of the exchange of the excited closed states are very different in the mutants, despite the similarities found in the ground states of the mutant and wild-types. There are 2 pathways, intrinsic and allosteric pathways that this enzyme can take depending on the environmental conditions. |
complete | |||||
enables |
GO:0070402 |
NADPH binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051870 |
methotrexate binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005542 |
folic acid binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0070401 |
NADP+ binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0005542 |
folic acid binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0070401 |
NADP+ binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051871 |
dihydrofolic acid binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0070402 |
NADPH binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0050661 |
NADP binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000167322 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0046655 |
folic acid metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000167322 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0046654 |
tetrahydrofolate biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000167322 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0046452 |
dihydrofolate metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000167322 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10326 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10326 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0042493 |
response to drug |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000314 |
direct assay 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 | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
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:0006730 |
one-carbon metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
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:0046677 |
response to antibiotic |
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.
- ↑ Oyen, D et al. (2015) Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway. J. Am. Chem. Soc. 137 9459-68 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Sawaya, MR & Kraut, J (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36 586-603 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 Schnell, JR et al. (2004) Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. Biochemistry 43 374-83 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Rood, JI et al. (1980) Cloning of the Escherichia coli K-12 dihydrofolate reductase gene following mu-mediated transposition. Gene 8 255-65 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
- ↑ Baccanari, D et al. (1975) Purification and properties of Escherichia coli dihydrofolate reductase. Biochemistry 14 5267-73 PubMed GONUTS page
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