Reviewed,
UniProtKB/Swiss-Prot Q6GGY1 (DYR_STAAR)
Last modified
February 9, 2010.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Dihydrofolate reductase Short name=DHFR EC=1.5.1.3 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282458 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 159 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
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 | |
| 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 |
| Technical term | 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 oxidation reductionInferred 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 159 | 158 | Dihydrofolate reductase | PRO_0000186409 | |||||
Regions | |||||||||
| Domain | 2 – 157 | 156 | DHFR | ||||||
| Nucleotide binding | 7 – 8 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 15 – 20 | 6 | NADP By similarity | ||||||
| Nucleotide binding | 44 – 47 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 63 – 66 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 93 – 98 | 6 | NADP By similarity | ||||||
| Region | 6 – 8 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 28 | 1 | Substrate By similarity | ||||||
| Binding site | 58 | 1 | Substrate By similarity | ||||||
| Binding site | 112 | 1 | Substrate By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571856 Genomic DNA. Translation: CAG40436.1. |
| RefSeq | YP_040841.1. |
3D structure databases | |
| SMR | Q6GGY1. Positions 1-159. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6GGY1. |
Genome annotation databases | |
| GeneID | 2859591. |
| GenomeReviews | Gene locus SAR1439 in contig BX571856_GR. |
| KEGG | sar:SAR1439. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0262. |
| HOGENOM | HBG665708. |
| OMA | GLPWHLP. |
Enzyme and pathway databases | |
| BioCyc | SAUR282458:SAR1439-MONOMER. |
Family and domain databases | |
| InterPro | IPR012259. DHFR. IPR017925. Dihydrofolate_reductase_CS. IPR001796. Dihydrofolate_reductase_dom. [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... |
Other Resources | |
| BindingDB | Q6GGY1. |
Entry information
| Entry name | DYR_STAAR | ||||||||
| Accession | Primary (citable) accession number: Q6GGY1 | ||||||||
| Entry history |
| ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


