Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A017 (DYR_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrofolate reductase

Short name=DHFR
EC=1.5.1.3
Gene names
Name:folA
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.

Miscellaneous

There are two DhfR isozymes in S.aureus, this one is chromosomal and is sensitive to trimethoprim.

Sequence similarities

Belongs to the dihydrofolate reductase family.

Contains 1 DHFR (dihydrofolate reductase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 159158Dihydrofolate reductase
PRO_0000186411

Regions

Domain2 – 157156DHFR
Nucleotide binding7 – 82NADP
Nucleotide binding15 – 206NADP
Nucleotide binding44 – 474NADP
Nucleotide binding63 – 664NADP
Nucleotide binding93 – 986NADP
Region6 – 83Substrate binding

Sites

Binding site281Substrate
Binding site581Substrate
Binding site1011NADP
Binding site1121Substrate
Binding site1221NADP

Secondary structure

.............................. 159
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A017 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 811898409FEAFAAB

FASTA15918,251
        10         20         30         40         50         60 
MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES IGKPLPNRRN 

        70         80         90        100        110        120 
VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE EMIDKVDDMY ITVIEGKFRG 

       130        140        150 
DTFFPPYTFE DWEVASSVEG KLDEKNTIPH TFLHLIRKK 

« Hide

References

[1]"Characterization of the gene for chromosomal trimethoprim-sensitive dihydrofolate reductase of Staphylococcus aureus ATCC 25923."
Dale G.E., Then R.L., Stueber D.
Antimicrob. Agents Chemother. 37:1400-1405(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.
[2]"N-terminal amino acid sequence of the chromosomal dihydrofolate reductase purified from trimethoprim-resistant Staphylococcus aureus."
Hartman P.G., Stahli M., Kocher H.P., Then R.L.
FEBS Lett. 242:157-160(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-36.
Strain: 157/4696.
[3]"Inhibitory properties and X-ray crystallographic study of the binding of AR-101, AR-102 and iclaprim in ternary complexes with NADPH and dihydrofolate reductase from Staphylococcus aureus."
Oefner C., Parisi S., Schulz H., Lociuro S., Dale G.E.
Acta Crystallogr. D 65:751-757(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-159.
[4]"Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim."
Heaslet H., Harris M., Fahnoe K., Sarver R., Putz H., Chang J., Subramanyam C., Barreiro G., Miller J.R.
Proteins 76:706-717(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH NADPH AND TRIMETHOPRIM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z16422 Genomic DNA. Translation: CAA78910.1.
PIRS32014.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W9GX-ray1.95A1-159[»]
2W9HX-ray1.48A1-159[»]
3FRAX-ray2.35X2-159[»]
3FRBX-ray2.00X2-159[»]
3FRDX-ray2.10X2-159[»]
3FREX-ray2.20X2-159[»]
3FRFX-ray2.20X2-159[»]
3FY8X-ray2.20X2-159[»]
3FY9X-ray2.25X2-159[»]
3FYVX-ray2.20X2-159[»]
3FYWX-ray2.10X2-159[»]
3I8AX-ray2.41X2-158[»]
3LG4X-ray3.15A/B1-158[»]
3M08X-ray2.01A2-158[»]
3M09X-ray2.01A2-158[»]
3SGYX-ray2.60A/B2-158[»]
3SH2X-ray3.00A/B2-158[»]
3SQYX-ray1.50X1-159[»]
3SR5X-ray1.68X2-159[»]
3SRQX-ray1.69X1-159[»]
3SRRX-ray1.70X1-159[»]
3SRSX-ray1.70X1-159[»]
3SRUX-ray1.70X1-159[»]
3SRWX-ray1.70X1-159[»]
4FGGX-ray2.30A1-159[»]
4FGHX-ray2.50A1-159[»]
4LAEX-ray1.69X1-159[»]
4LAGX-ray1.70X1-159[»]
4LAHX-ray1.88X1-159[»]
4LEKX-ray1.70X1-159[»]
ProteinModelPortalP0A017.
SMRP0A017. Positions 2-158.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP0A017.
ChEMBLCHEMBL1681620.

Proteomic databases

PRIDEP0A017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0262.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFPIRSF000194. DHFR. 1 hit.
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A017.

Entry information

Entry nameDYR_STAAU
AccessionPrimary (citable) accession number: P0A017
Secondary accession number(s): P10167
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways