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Reviewed, UniProtKB/Swiss-Prot P00378 (DYR_CHICK)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrofolate reductase
    EC=1.5.1.3
Gene names
Name: DHFR
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.

Miscellaneous

The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

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

Experimental info

Sequence conflict1411E → Q AA sequence Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00378-1 [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: 6766736] [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: 8670138] [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: 1510919] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

IPIIPI00822128.
PIRRDCHD. A00390.
UniGeneGga.2883

3D structure databases

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[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSGALG00000015579. Gallus gallus. [Contig view]

Phylogenomic databases

HOGENOMP00378.
HOVERGENP00378.

Enzyme and pathway databases

BRENDA1.5.1.3. 4.

Family and domain databases

InterProIPR012259. DHFR.
IPR001796. DHFR_reg.
IPR017925. Dihydrofolate_reductase_CS.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents