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

P00380 (DYR_ENTFC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=1.5.1.3
Gene names
Name:folA
OrganismEnterococcus faecium (Streptococcus faecium)
Taxonomic identifier1352 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length167 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.

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 – 167167Dihydrofolate reductase
PRO_0000186390

Regions

Domain1 – 162162DHFR
Nucleotide binding13 – 197NADP By similarity
Nucleotide binding45 – 462NADP By similarity
Nucleotide binding64 – 652NADP By similarity
Nucleotide binding99 – 1068NADP By similarity

Sites

Binding site71NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site271Substrate By similarity
Binding site581Substrate By similarity
Binding site1171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P00380 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E00C2CF3BC420585

FASTA16719,583
        10         20         30         40         50         60 
MFISMWAQDK NGLIGKDGLL PWRLPNDMRF FREHTMDKIL VMGRKTYEGM GKLSLPYRHI 

        70         80         90        100        110        120 
IVLTTQKDFK VEKNAEVLHS IDELLAYAKD IPEDIYVSGG SRIFQALLPE TKIIWRTLID 

       130        140        150        160 
AEFEGDTFIG EIDFTSFELV EEHEGIVNQE NQYPHRFQKW QKMSKVV 

« Hide

References

[1]"The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the protein."
Peterson D.L., Gleisner J.M., Blakley R.L.
J. Biol. Chem. 250:4945-4954(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: A / var. Durans.

Cross-references

Sequence databases

PIRRDSODF. A00392.

3D structure databases

ProteinModelPortalP00380.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameDYR_ENTFC
AccessionPrimary (citable) accession number: P00380
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2013
This is version 73 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways