Reviewed,
UniProtKB/Swiss-Prot P04382 (DYR_BPT4)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dihydrofolate reductase EC=1.5.1.3 | ||
| Gene names |
| ||
| Organism | Enterobacteria phage T4 (Bacteriophage T4) | ||
| Taxonomic identifier | 10665 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › T4-like viruses | ||
| Virus host | Escherichia coli [TaxID: 562] |
Protein attributes
| Sequence length | 193 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. |
| 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 | Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance Methotrexate resistance One-carbon metabolism Trimethoprim resistance |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic processInferred from electronic annotation. Source: InterPro one-carbon compound metabolic processInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW response to antibioticInferred from electronic annotation. Source: UniProtKB-KW response to methotrexateInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 193 | 193 | Dihydrofolate reductase | PRO_0000186434 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Domain | 1 – 193 | 193 | DHFR | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 2 – 12 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 18 – 24 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 34 – 44 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 47 – 52 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 53 – 57 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 71 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 88 – 91 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 100 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 108 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 115 – 118 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 124 – 128 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 130 – 136 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 137 – 139 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 141 – 152 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 157 – 160 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 162 – 169 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 173 – 182 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 185 – 192 | 8 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence reveals overlap between T4 phage genes encoding dihydrofolate reductase and thymidylate synthase." Purohit S., Mathews C.K. J. Biol. Chem. 259:6261-6266(1984) [PubMed: 6327673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Bacteriophage T4 genome." Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W. Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed: 12626685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "Characterization of the intron in the phage T4 thymidylate synthase gene and evidence for its self-excision from the primary transcript." Chu F.K., Maley G.F., West D.K., Belfort M., Maley F. Cell 45:157-166(1986) [PubMed: 3698096] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-193. Strain: ALC4. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| K01804 Genomic DNA. Translation: AAA32491.1. AF158101 Genomic DNA. Translation: AAD42577.1. M12742 Genomic DNA. Translation: AAC12815.1. | |||||||||||||
| PIR | RDBPT4. A00396. | ||||||||||||
| RefSeq | NP_049850.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1258671. | ||||||||||||
| GenomeReviews | Gene locus T4p240 in contig AF158101_GR. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.5.1.3. 1108. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR012259. DHFR. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. [Graphical view] | ||||||||||||
| PANTHER | PTHR11549:SF1. DHFR. 1 hit. | ||||||||||||
| Pfam | PF00186. DHFR_1. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00070. DHFR. | ||||||||||||
| PROSITE | PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | DYR_BPT4 | ||||||||
| Accession | Primary (citable) accession number: P04382 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


