Q54801 (DYR_STRPN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dihydrofolate reductase EC=1.5.1.3 | ||||||
| Gene names |
| ||||||
| Organism | Streptococcus pneumoniae [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1313 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 168 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity. |
| Catalytic activity | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. |
| Pathway | |
| Miscellaneous | Strains 1/1, 21, 30, 56 and 92 are trimethoprim resistant. |
| Sequence similarities | Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance One-carbon metabolism Trimethoprim resistance |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic processInferred from electronic annotation. Source: InterPro one-carbon metabolic processInferred from electronic annotation. Source: UniProtKB-KW response to antibioticInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NADP 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 – 168 | 168 | Dihydrofolate reductase | PRO_0000186417 | ||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||
| Domain | 4 – 165 | 162 | DHFR | |||||||||||||||||||||||||||||||
| Nucleotide binding | 9 – 10 | 2 | NADP By similarity | |||||||||||||||||||||||||||||||
| Nucleotide binding | 17 – 22 | 6 | NADP By similarity | |||||||||||||||||||||||||||||||
| Nucleotide binding | 46 – 49 | 4 | NADP By similarity | |||||||||||||||||||||||||||||||
| Nucleotide binding | 66 – 69 | 4 | NADP By similarity | |||||||||||||||||||||||||||||||
| Nucleotide binding | 100 – 105 | 6 | NADP By similarity | |||||||||||||||||||||||||||||||
| Region | 8 – 10 | 3 | Substrate binding By similarity | |||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||
| Binding site | 30 | 1 | Substrate By similarity | |||||||||||||||||||||||||||||||
| Binding site | 61 | 1 | Substrate By similarity | |||||||||||||||||||||||||||||||
| Binding site | 83 | 1 | NADP; via amide nitrogen By similarity | |||||||||||||||||||||||||||||||
| Binding site | 119 | 1 | Substrate By similarity | |||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||
| Natural variant | 14 | 1 | E → D in strain: 21. | |||||||||||||||||||||||||||||||
| Natural variant | 20 | 1 | E → D in strain: 21, 30 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 60 | 1 | K → Q in strain: 30, 56 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 65 | 1 | I → V in strain: 92. | |||||||||||||||||||||||||||||||
| Natural variant | 70 | 1 | P → S in strain: 21, 56 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 74 | 1 | I → L in strain: 21. | |||||||||||||||||||||||||||||||
| Natural variant | 77 – 78 | 2 | VA → AV in strain: 30. | |||||||||||||||||||||||||||||||
| Natural variant | 81 | 1 | Q → H in strain: 21, 56 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 91 | 1 | Q → H in strain: 21. | |||||||||||||||||||||||||||||||
| Natural variant | 92 | 1 | A → D in strain: ATCC 49619. | |||||||||||||||||||||||||||||||
| Natural variant | 94 | 1 | E → D in strain: 21. | |||||||||||||||||||||||||||||||
| Natural variant | 100 | 1 | I → L in strain: 21, 30, 56 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 111 | 1 | P → S in strain: 56 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 135 | 1 | L → F in strain: 21, 30, 56 and 1/1. | |||||||||||||||||||||||||||||||
| Natural variant | 141 | 1 | E → D in strain: 56. | |||||||||||||||||||||||||||||||
| Natural variant | 147 – 149 | 3 | FYA → SYT in strain: 21. | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 11 | 7 | ||||||||||||||||||||||||||||||||
| Helix | 28 – 38 | 11 | ||||||||||||||||||||||||||||||||
| Beta strand | 41 – 45 | 5 | ||||||||||||||||||||||||||||||||
| Turn | 48 – 50 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 62 – 66 | 5 | ||||||||||||||||||||||||||||||||
| Beta strand | 78 – 82 | 5 | ||||||||||||||||||||||||||||||||
| Helix | 83 – 91 | 9 | ||||||||||||||||||||||||||||||||
| Beta strand | 97 – 99 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 104 – 109 | 6 | ||||||||||||||||||||||||||||||||
| Helix | 110 – 112 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 114 – 123 | 10 | ||||||||||||||||||||||||||||||||
| Helix | 137 – 139 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 140 – 148 | 9 | ||||||||||||||||||||||||||||||||
| Beta strand | 158 – 165 | 8 | ||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | Caspers P. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 49619 / 262 / CIP 104340 / Serotype 19F and Trimethoprim resistant 1/1 Johannesburg 1993. |
| [2] | "Mutations in the dihydrofolate reductase gene of trimethoprim-resistant isolates of Streptococcus pneumoniae." Adrian P.V., Klugman K.P. Antimicrob. Agents Chemother. 41:2406-2413(1997) [PubMed: 9371341] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 30, 56, 92 and Trimethoprim resistant 21. |
| [3] | "Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. Fraser C.M.Science 293:498-506(2001) [PubMed: 11463916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | Z74777 Genomic DNA. Translation: CAA99035.1. Z74778 Genomic DNA. Translation: CAA99036.1. Z84378 Genomic DNA. Translation: CAB06418.1. Z84379 Genomic DNA. Translation: CAB06419.1. Z84380 Genomic DNA. Translation: CAB06420.1. Z84381 Genomic DNA. Translation: CAB06421.1. AE005672 Genomic DNA. Translation: AAK75658.1. | ||||||||||||
| PIR | A95183. | ||||||||||||
| RefSeq | NP_346018.1. NC_003028.3. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q54801. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBSTRT00000026574; EBSTRP00000025666; EBSTRG00000026574. | ||||||||||||
| GeneID | 931270. | ||||||||||||
| GenomeReviews | Gene locus SP_1571 in contig AE005672_GR. | ||||||||||||
| KEGG | spn:SP_1571. | ||||||||||||
| PATRIC | 19707567. VBIStrPne105772_1626. | ||||||||||||
| TIGR | SP_1571. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | EBGT00050000027355. | ||||||||||||
| HOGENOM | HBG665708. | ||||||||||||
| OMA | QDEEGVI. | ||||||||||||
| ProtClustDB | CLSK884121. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | SPNE170187-1:SP_1571-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR012259. DHFR. IPR024072. DHFR-like_dom. IPR017925. DHFR_CS. IPR001796. DHFR_dom. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit. | ||||||||||||
| KO | K00287. | ||||||||||||
| PANTHER | PTHR11549:SF1. DHFR. 1 hit. | ||||||||||||
| Pfam | PF00186. DHFR_1. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF000194. DHFR. 1 hit. | ||||||||||||
| PRINTS | PR00070. DHFR. | ||||||||||||
| SUPFAM | SSF53597. SSF53597. 1 hit. | ||||||||||||
| PROSITE | PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| BindingDB | Q54801. | ||||||||||||
Entry information
| Entry name | DYR_STRPN | ||||||||
| Accession | Primary (citable) accession number: Q54801 Secondary accession number(s): O08440 Q54973 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
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