Reviewed,
UniProtKB/Swiss-Prot P00384 (DYR22_ECOLX)
Last modified
November 25, 2008.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dihydrofolate reductase type 2 EC=1.5.1.3 Alternative name(s): Dihydrofolate reductase type II |
| Encoded on | Plasmid IncW R388 |
| Organism | Escherichia coli |
| Taxonomic identifier | 562 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 78 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Predicted. |
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 | Type II plasmid-specified enzyme is practically insensitive to trimethoprim and methotrexate. 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. |
Ontologies
Keywords | |
|---|---|
| Biological process | Antibiotic resistance Methotrexate resistance One-carbon metabolism Trimethoprim resistance |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Plasmid |
Gene Ontology (GO) | |
| Biological process | one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW photosynthesisInferred from electronic annotation. Source: InterPro response to antibioticInferred from electronic annotation. Source: UniProtKB-KW response to drugInferred from electronic annotation. Source: InterPro response to methotrexateInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plastid Inferred from electronic annotation. Source: InterPro |
| Molecular function | dihydrofolate reductase activity Inferred 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 – 78 | 78 | Dihydrofolate reductase type 2 | PRO_0000186436 | |||
Sequences
References
| [1] | "Characterization of a R plasmid-associated, trimethoprim-resistant dihydrofolate reductase and determination of the nucleotide sequence of the reductase gene." Zolg J.W., Haenggi U.J. Nucleic Acids Res. 9:697-710(1981) [PubMed: 6261228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "DNA sequence of a plasmid-encoded dihydrofolate reductase." Swift G., McCarthy B.J., Heffron F. Mol. Gen. Genet. 181:441-447(1981) [PubMed: 7022127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| V00252 Genomic DNA. Translation: CAA23503.1. J01773 Genomic DNA. Translation: AAA72145.1. | |
| PIR | RDECD8. A00398. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1VIE based on UniProtKB P00383. |
| SMR | P00384. Positions 19-77. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR009159. Dhfr_type_II. [Graphical view] |
| Pfam | PF06442. DHFR_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000199. Dhfr_type_II. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DYR22_ECOLX | ||||||||
| Accession | Primary (citable) accession number: P00384 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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