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P00378 (DYR_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 105. 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

EC=1.5.1.3
Gene names
Name:DHFR
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. May bind to mRNA.

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 – 189189Dihydrofolate reductase
PRO_0000186367

Regions

Domain3 – 184182DHFR
Nucleotide binding15 – 217NADP
Nucleotide binding54 – 563NADP
Nucleotide binding76 – 783NADP
Nucleotide binding116 – 1238NADP
Region30 – 356Substrate binding

Sites

Binding site91NADP; via amide nitrogen and carbonyl oxygen
Binding site701Substrate

Experimental info

Sequence conflict1411E → Q AA sequence Ref.2

Secondary structure

................................... 189
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00378 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: BC5F50C94BCA3EDA

FASTA18921,650
        10         20         30         40         50         60 
VRSLNSIVAV CQNMGIGKDG NLPWPPLRNE YKYFQRMTST SHVEGKQNAV IMGKKTWFSI 

        70         80         90        100        110        120 
PEKNRPLKDR INIVLSRELK EAPKGAHYLS KSLDDALALL DSPELKSKVD MVWIVGGTAV 

       130        140        150        160        170        180 
YKAAMEKPIN HRLFVTRILH EFESDTFFPE IDYKDFKLLT EYPGVPADIQ EEDGIQYKFE 


VYQKSVLAQ 

« Hide

References

[1]"Primary structure of chicken liver dihydrofolate reductase."
Kumar A.A., Blankenship D.T., Kaufman B.T., Freisheim J.H.
Biochemistry 19:667-678(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site."
Fan Y.X., Ju M., Zhou J.M., Tsou C.L.
Biochem. J. 315:97-102(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-22; 138-141 AND 158-161.
[3]"Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin."
McTigue M.A., Davies J.F. II, Kaufman B.T., Kraut J.
Biochemistry 31:7264-7273(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH NADPH AND DIHYDROBIOPTERIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRRDCHD. A00390.
UniGeneGga.2883.
Gga.48831.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DR1X-ray2.20A1-189[»]
1DR2X-ray2.30A1-189[»]
1DR3X-ray2.30A1-189[»]
1DR4X-ray2.40A1-189[»]
1DR5X-ray2.40A1-189[»]
1DR6X-ray2.40A1-189[»]
1DR7X-ray2.40A1-189[»]
8DFRX-ray1.70A1-189[»]
ProteinModelPortalP00378.
SMRP00378. Positions 1-186.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00378.
ChEMBLCHEMBL2575.

Proteomic databases

PaxDbP00378.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0262.
HOVERGENHBG000773.
InParanoidP00378.

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]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00378.
PROP00378.

Entry information

Entry nameDYR_CHICK
AccessionPrimary (citable) accession number: P00378
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 22, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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