Reviewed,
UniProtKB/Swiss-Prot P0C0P0 (DYR_STAEP)
Last modified
November 25, 2008.
Version 18.
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 Short name=DHFR EC=1.5.1.3 | ||||
| Gene names |
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| Organism | Staphylococcus epidermidis | ||||
| Taxonomic identifier | 1282 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 161 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Not resistant to trimethoprim. |
| 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 | One-carbon metabolism |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
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 |
| Molecular function | NADP binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase 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 – 161 | 161 | Dihydrofolate reductase | PRO_0000186413 | |||||
Regions | |||||||||
| Domain | 2 – 157 | 156 | DHFR | ||||||
Experimental info | |||||||||
| Mutagenesis | 32 | 1 | V → I: 3-fold increase of KM for dihydrofolate | ||||||
| Mutagenesis | 44 | 1 | G → A: 5-fold increase of KM for NADPH | ||||||
| Mutagenesis | 99 | 1 | F → Y: Trimethoprim resistance | ||||||
Sequences
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References
| [1] | "Characterization of the gene for the chromosomal dihydrofolate reductase (DHFR) of Staphylococcus epidermidis ATCC 14990: the origin of the trimethoprim-resistant S1 DHFR from Staphylococcus aureus?" Dale G.E., Broger C., Hartman P.G., Langen H., Page M.G.P., Then R.L., Stueber D. J. Bacteriol. 177:2965-2970(1995) [PubMed: 7768789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS. Strain: ATCC 14990 / DSM 20044 / CIP 81.55. |
Cross-references
Sequence databases | |
|---|---|
| Z48233 Genomic DNA. Translation: CAA88269.1. | |
| PIR | A57271. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DHI based on UniProtKB P00379. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR012259. DHFR. IPR001796. DHFR_reg. [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_STAEP | ||||||||
| Accession | Primary (citable) accession number: P0C0P0 Secondary accession number(s): Q59908 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
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 |

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