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P0C0P0 (DYR_STAEP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrofolate reductase
Short name=DHFR
EC=1.5.1.3
Gene names
Name:folA
Synonyms:dfrC, folA1
OrganismStaphylococcus epidermidis
Taxonomic identifier1282 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
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 By similarity.

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

Trimethoprim sensitive.

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

Chain1 – 161161Dihydrofolate reductase
PRO_0000186413

Regions

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

Sites

Binding site281Substrate By similarity
Binding site581Substrate By similarity
Binding site1121Substrate By similarity

Experimental info

Mutagenesis321V → I: 3-fold increase of KM for dihydrofolate.
Mutagenesis441G → A: 5-fold increase of KM for NADPH.
Mutagenesis991F → Y: Trimethoprim resistance.

Sequences

Sequence LengthMass (Da)Tools
P0C0P0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: CB3167940A387EE0

FASTA16118,417
        10         20         30         40         50         60 
MTLSIIVAHD KQRVIGYQNQ LPWHLPNDLK HVKQLTTGNT LVMGRKTFNS IGKPLPNRRN 

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

       130        140        150        160 
DTFFPPYTFE NWEVESSVEG QLDEKNTIPH TFLHLVRRKG K

« Hide

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

EMBL
GenBank
DDBJ		Z48233 Genomic DNA. Translation: CAA88269.1.
PIRA57271.

3D structure databases

ProteinModelPortalP0C0P0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
Gene3DG3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit.
PANTHERPTHR11549:SF1. DHFR. 1 hit.
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...

Entry information

Entry nameDYR_STAEP
AccessionPrimary (citable) accession number: P0C0P0
Secondary accession number(s): Q59908
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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