Reviewed,
UniProtKB/Swiss-Prot Q27713 (DRTS_PLABA)
Last modified
November 25, 2008.
Version 47.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional dihydrofolate reductase-thymidylate synthase Short name=DHFR-TS Including the following 2 domains: 1- Recommended name: Dihydrofolate reductase EC=1.5.1.3 2- Recommended name: Thymidylate synthase EC=2.1.1.45 |
| Organism | Plasmodium berghei (strain Anka) |
| Taxonomic identifier | 5823 [NCBI] |
| Taxonomic lineage | Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Vinckeia) |
Protein attributes
| Sequence length | 587 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. |
| Pathway | Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1. |
| Miscellaneous | The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. |
| Sequence similarities | In the N-terminal section; belongs to the dihydrofolate reductase family. In the C-terminal section; belongs to the thymidylate synthase family. Contains 1 DHFR (dihydrofolate reductase) domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Nucleotide biosynthesis One-carbon metabolism |
| Ligand | NADP |
| Molecular function | Methyltransferase Oxidoreductase Transferase |
| Technical term | Multifunctional enzyme |
Gene Ontology (GO) | |
| Biological process | dTMP biosynthetic process Inferred from electronic annotation. Source: InterPro glycine biosynthetic processInferred from electronic annotation. Source: InterPro one-carbon compound metabolic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | dihydrofolate reductase activity Inferred from electronic annotation. Source: InterPro thymidylate synthase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 587 | 587 | Bifunctional dihydrofolate reductase-thymidylate synthase | PRO_0000186347 | |||||
Regions | |||||||||
| Domain | 9 – 237 | 229 | DHFR | ||||||
| Region | 301 – 587 | 287 | Thymidylate synthase | ||||||
Sites | |||||||||
| Active site | 469 | 1 | By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 110 | 1 | S → N in pyrimethamine resistance. | ||||||
| Natural variant | 177 | 1 | S → F in pyrimethamine resistance. | ||||||
Sequences
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References
| [1] | "Mechanisms of pyrimethamine resistance in two different strains of Plasmodium berghei." van Dijk M.R., McConkey G.A., Vinkenoog R., Waters A.P., Janse C.J. Mol. Biochem. Parasitol. 68:167-171(1994) [PubMed: 7891743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The dihydrofolate reductase domain of rodent malarias: point mutations and pyrimethamine resistance." Cheng Q., Saul A. Mol. Biochem. Parasitol. 65:361-363(1994) [PubMed: 7969277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-201. |
Cross-references
Sequence databases | |
|---|---|
| U12275 Genomic DNA. Translation: AAB60237.1. L28119 Genomic DNA. Translation: AAA29581.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1J3K based on UniProtKB P13922. |
| SMR | Q27713. Positions 264-587. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR012262. DHFR-TS. IPR001796. DHFR_reg. IPR000398. Thymidylat_synth_C. [Graphical view] |
| Gene3D | G3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit. |
| PANTHER | PTHR11549:SF2. Thymidylat_synth_C. 1 hit. |
| Pfam | PF00186. DHFR_1. 1 hit. PF00303. Thymidylat_synt. 1 hit. [Graphical view] |
| PIRSF | PIRSF000389. DHFR-TS. 1 hit. |
| PRINTS | PR00070. DHFR. PR00108. THYMDSNTHASE. |
| ProDom | PD001180. Thymidylat_synth. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR03284. thym_sym. 1 hit. |
| PROSITE | PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. PS00091. THYMIDYLATE_SYNTHASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00440. Trimethoprim. |
Entry information
| Entry name | DRTS_PLABA | ||||||||
| Accession | Primary (citable) accession number: Q27713 Secondary accession number(s): Q27714 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


