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P13955 (DYRA_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 89. 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 type 1 from Tn4003

EC=1.5.1.3
Gene names
Name:dfrA
Encoded onPlasmid pSK1
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length161 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 plasmid-encoded and is resistant 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 By similarity
Chain2 – 161160Dihydrofolate reductase type 1 from Tn4003
PRO_0000186405

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 site1121Substrate

Experimental info

Mutagenesis441A → G: Increases trimethoprim sensitivity; when associated with F-99. Ref.3
Mutagenesis991Y → F: Increases trimethoprim sensitivity; when associated with G-44. Ref.3

Secondary structure

................................ 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13955 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F829D6109A3AF3A0

FASTA16118,461
        10         20         30         40         50         60 
MTLSIIVAHD KQRVIGYQNQ LPWHLPNDLK HIKQLTTGNT LVMARKTFNS IGKPLPNRRN 

        70         80         90        100        110        120 
VVLTNQASFH HEGVDVINSL DEIKELSGHV FIFGGQTLYE AMIDQVDDMY ITVIDGKFQG 

       130        140        150        160 
DTFFPPYTFE NWEVESSVEG QLDEKNTIPH TFLHLVRRKG K 

« Hide

References

[1]"Trimethoprim resistance transposon Tn4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS257."
Rouch D.A., Messeroti L.J., Loo L.S.L., Jackson C.A., Skurray R.A.
Mol. Microbiol. 3:161-175(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Transposon: Tn4003.
[2]"Identical genes for trimethoprim-resistant dihydrofolate reductase from Staphylococcus aureus in Australia and central Europe."
Burdeska A., Ott M., Bannwarth W., Then R.L.
FEBS Lett. 266:159-162(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 157/4696.
[3]"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 (1.8 ANGSTROMS) IN COMPLEX WITH NADPH AND TRIMETHOPRIM, MUTAGENESIS OF ALA-44 AND TYR-99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13290 Genomic DNA. Translation: CAA31649.1.
Y07536 Genomic DNA. Translation: CAA68824.1.
PIRS04164.
RefSeqNP_877983.1. NC_005054.1.
YP_002790943.1. NC_012547.1.
YP_003813115.1. NC_014369.1.
YP_006937652.1. NC_013320.1.
YP_006937707.1. NC_013321.1.
YP_006938354.1. NC_013338.1.
YP_006938562.1. NC_013343.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W9SX-ray1.80A/B/C/D/E/F1-161[»]
2W9TX-ray2.35A/B1-161[»]
ProteinModelPortalP13955.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP13955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13874802.
13874858.
13875495.
13875735.
2598376.
7751508.
9487075.

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

EvolutionaryTraceP13955.

Entry information

Entry nameDYRA_STAAU
AccessionPrimary (citable) accession number: P13955
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 89 of the entry and version 3 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