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9CAUD:A0A0K2D000
Contents
Species (Taxon ID) | Bacillus phage TsarBomba. (1690456) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Dihydrofolate reductase (ECO:0000313 with EMBL:ALA13144.1) | |
External Links | ||
UniProt | A0A0K2D000 | |
EMBL | KT224359 | |
RefSeq | YP_009206863.1 | |
GeneID | 26633354 | |
GO | GO:0004146 GO:0050661 GO:0006545 GO:0009165 | |
Gene3D | 3.40.430.10 | |
InterPro | IPR012259 IPR024072 IPR001796 | |
Pfam | PF00186 | |
PIRSF | PIRSF000194 | |
PRINTS | PR00070 | |
SUPFAM | SSF53597 | |
PROSITE | 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:0000250 |
|
F |
Transfer annotation from gene page ECOLI:DYR. With an E value of 2e-35, there is strong support for sequence similarity (accession #: 5CC9_A). |
complete | ||||
GO:0050661 |
NADP binding |
ECO:0000250 |
|
F |
Transfer annotation from gene page LACCA:DYR. Strong sequence similarity with an E value of 2E-34. Accession #: 4DFR_A |
complete | ||||
GO:0004146 |
dihydrofolate reductase activity |
ECO:0000250 |
|
F |
With an E value of 1e-14, there is strong support for sequence similarity (accession #: WP_010865375.1). |
complete | ||||
GO:0004146 |
dihydrofolate reductase activity |
other:GO_REF:0000100 |
ECO:0000247 |
UniProtKB:A0A0K2D000_9CAUD
|
F |
The blast data for this sequence from Eyuki matches the diydrofolate reductase gene on TsarBomba. This data shows an e-value of 7e-41, an identity match of 46%, and a coverage of 98%. |
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 | |||
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
- ↑ 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
- ↑ Dams, T et al. (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability. J. Mol. Biol. 297 659-72 PubMed GONUTS page
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