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P17719 (DYR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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
ORF Names:CG14887
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length182 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

By interacting with vestigial (vg), may control genes involved in DNA replication.

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.

Subunit structure

Monomer. Interacts with vg. Ref.5

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 – 182182Dihydrofolate reductase
PRO_0000186370

Regions

Domain3 – 180178DHFR
Nucleotide binding15 – 217NADP By similarity
Nucleotide binding53 – 553NADP By similarity
Nucleotide binding75 – 773NADP By similarity
Nucleotide binding113 – 1208NADP By similarity
Region29 – 346Substrate binding By similarity

Sites

Binding site91NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site691Substrate By similarity

Experimental info

Sequence conflict31R → T AA sequence Ref.4
Sequence conflict111C → S AA sequence Ref.4
Sequence conflict1341K → Q in AAA19051. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17719 [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: D2C9198F1D2CE430

FASTA18220,775
        10         20         30         40         50         60 
MLRFNLIVAV CENFGIGIRG DLPWRIKSEL KYFSRTTKRT SDPTKQNAVV MGRKTYFGVP 

        70         80         90        100        110        120 
ESKRPLPDRL NIVLSTTLQE SDLPKGVLLC PNLETAMKIL EEQNEVENIW IVGGSGVYEE 

       130        140        150        160        170        180 
AMASPRCHRL YITKIMQKFD CDTFFPAIPD SFREVAPDSD MPLGVQEENG IKFEYKILEK 


HS 

« Hide

References

« Hide 'large scale' references
[1]"Dihydrofolate reductase of Drosophila. Cloning and expression of a gene with a rare transcript."
Hao H., Tyshenko M.G., Walker V.K.
J. Biol. Chem. 269:15179-15185(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 155-176.
Strain: Canton-S.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"The purification of dihydrofolate reductase from Drosophila melanogaster."
Rancourt S.L., Walker V.K.
Biochim. Biophys. Acta 1039:261-268(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-23.
Strain: Canton-S.
[5]"The Drosophila wing differentiation factor vestigial-scalloped is required for cell proliferation and cell survival at the dorso-ventral boundary of the wing imaginal disc."
Delanoue R., Legent K., Godefroy N., Flagiello D., Dutriaux A., Vaudin P., Becker J.L., Silber J.
Cell Death Differ. 11:110-122(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VG, INVOLVEMENT IN DNA REPLICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U06861 Unassigned DNA. Translation: AAA19051.1.
AE014297 Genomic DNA. Translation: AAF55324.1.
AE014297 Genomic DNA. Translation: ABI31175.1.
PIRA53803.
A33105. S10759.
RefSeqNP_001036720.1. NM_001043255.2.
NP_732147.1. NM_169721.2.
UniGeneDm.8025.

3D structure databases

ProteinModelPortalP17719.
SMRP17719. Positions 4-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67048. 3 interactions.
DIPDIP-20310N.
IntActP17719. 1 interaction.
MINTMINT-323567.
STRING7227.FBpp0082746.

Proteomic databases

PaxDbP17719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083295; FBpp0082746; FBgn0004087.
FBtr0110910; FBpp0110210; FBgn0004087.
GeneID42003.
KEGGdme:Dmel_CG14887.

Organism-specific databases

CTD1719.
FlyBaseFBgn0004087. Dhfr.

Phylogenomic databases

eggNOGCOG0262.
GeneTreeENSGT00390000010283.
InParanoidP17719.
KOK00287.
OMALPWHPIR.
OrthoDBEOG7V1FS3.
PhylomeDBP17719.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Gene expression databases

BgeeP17719.

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

GenomeRNAi42003.
NextBio826685.
PROP17719.

Entry information

Entry nameDYR_DROME
AccessionPrimary (citable) accession number: P17719
Secondary accession number(s): A4V302, Q9VEU4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase