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P17719

- DYR_DROME

UniProt

P17719 - DYR_DROME

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Protein

Dihydrofolate reductase

Gene

Dhfr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei69 – 691SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 217NADPBy similarity
Nucleotide bindingi53 – 553NADPBy similarity
Nucleotide bindingi75 – 773NADPBy similarity
Nucleotide bindingi113 – 1208NADPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: FlyBase
  2. NADP binding Source: InterPro

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. glycine biosynthetic process Source: InterPro
  3. nucleotide biosynthetic process Source: InterPro
  4. one-carbon metabolic process Source: UniProtKB-KW
  5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication, One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:Dhfr
ORF Names:CG14887
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004087. Dhfr.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 182182Dihydrofolate reductasePRO_0000186370Add
BLAST

Proteomic databases

PaxDbiP17719.

Expressioni

Gene expression databases

BgeeiP17719.
ExpressionAtlasiP17719. differential.

Interactioni

Subunit structurei

Monomer. Interacts with vg.1 Publication

Protein-protein interaction databases

BioGridi67048. 3 interactions.
DIPiDIP-20310N.
IntActiP17719. 1 interaction.
MINTiMINT-323567.
STRINGi7227.FBpp0082746.

Structurei

3D structure databases

ProteinModelPortaliP17719.
SMRiP17719. Positions 4-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 180178DHFRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 346Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0262.
GeneTreeiENSGT00390000010283.
InParanoidiP17719.
KOiK00287.
OMAiLPWHPIR.
OrthoDBiEOG7V1FS3.
PhylomeDBiP17719.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17719-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRFNLIVAV CENFGIGIRG DLPWRIKSEL KYFSRTTKRT SDPTKQNAVV
60 70 80 90 100
MGRKTYFGVP ESKRPLPDRL NIVLSTTLQE SDLPKGVLLC PNLETAMKIL
110 120 130 140 150
EEQNEVENIW IVGGSGVYEE AMASPRCHRL YITKIMQKFD CDTFFPAIPD
160 170 180
SFREVAPDSD MPLGVQEENG IKFEYKILEK HS
Length:182
Mass (Da):20,775
Last modified:June 1, 2001 - v3
Checksum:iD2C9198F1D2CE430
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31R → T AA sequence (PubMed:2116172)Curated
Sequence conflicti11 – 111C → S AA sequence (PubMed:2116172)Curated
Sequence conflicti134 – 1341K → Q in AAA19051. (PubMed:8195153)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06861 Unassigned DNA. Translation: AAA19051.1.
AE014297 Genomic DNA. Translation: AAF55324.1.
AE014297 Genomic DNA. Translation: ABI31175.1.
PIRiA53803.
S10759. A33105.
RefSeqiNP_001036720.1. NM_001043255.2.
NP_732147.1. NM_169721.2.
UniGeneiDm.8025.

Genome annotation databases

EnsemblMetazoaiFBtr0083295; FBpp0082746; FBgn0004087.
FBtr0110910; FBpp0110210; FBgn0004087.
GeneIDi42003.
KEGGidme:Dmel_CG14887.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06861 Unassigned DNA. Translation: AAA19051.1 .
AE014297 Genomic DNA. Translation: AAF55324.1 .
AE014297 Genomic DNA. Translation: ABI31175.1 .
PIRi A53803.
S10759. A33105.
RefSeqi NP_001036720.1. NM_001043255.2.
NP_732147.1. NM_169721.2.
UniGenei Dm.8025.

3D structure databases

ProteinModelPortali P17719.
SMRi P17719. Positions 4-180.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67048. 3 interactions.
DIPi DIP-20310N.
IntActi P17719. 1 interaction.
MINTi MINT-323567.
STRINGi 7227.FBpp0082746.

Proteomic databases

PaxDbi P17719.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0083295 ; FBpp0082746 ; FBgn0004087 .
FBtr0110910 ; FBpp0110210 ; FBgn0004087 .
GeneIDi 42003.
KEGGi dme:Dmel_CG14887.

Organism-specific databases

CTDi 1719.
FlyBasei FBgn0004087. Dhfr.

Phylogenomic databases

eggNOGi COG0262.
GeneTreei ENSGT00390000010283.
InParanoidi P17719.
KOi K00287.
OMAi LPWHPIR.
OrthoDBi EOG7V1FS3.
PhylomeDBi P17719.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Miscellaneous databases

GenomeRNAii 42003.
NextBioi 826685.
PROi P17719.

Gene expression databases

Bgeei P17719.
ExpressionAtlasi P17719. differential.

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiDYR_DROME
AccessioniPrimary (citable) accession number: P17719
Secondary accession number(s): A4V302, Q9VEU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3