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Protein

Dihydrofolate reductase

Gene

DFR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 sitei13 – 131NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei74 – 741SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 267NADPBy similarity
Nucleotide bindingi58 – 603NADPBy similarity
Nucleotide bindingi80 – 823NADPBy similarity
Nucleotide bindingi123 – 1308NADPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: SGD
  2. mRNA binding Source: SGD
  3. NADP binding Source: InterPro

GO - Biological processi

  1. dihydrofolate metabolic process Source: SGD
  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: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:YOR236W-MONOMER.
ReactomeiREACT_303865. E2F mediated regulation of DNA replication.
REACT_324954. Metabolism of folate and pterines.
REACT_342867. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_345909. G1/S-Specific Transcription.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:DFR1
Ordered Locus Names:YOR236W
ORF Names:O5231
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR236w.
SGDiS000005762. DFR1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Dihydrofolate reductasePRO_0000186378Add
BLAST

Proteomic databases

MaxQBiP07807.
PaxDbiP07807.
PRIDEiP07807.

Expressioni

Gene expression databases

GenevestigatoriP07807.

Interactioni

Protein-protein interaction databases

BioGridi34628. 45 interactions.
DIPiDIP-4120N.
IntActiP07807. 4 interactions.
MINTiMINT-532257.
STRINGi4932.YOR236W.

Structurei

3D structure databases

ProteinModelPortaliP07807.
SMRiP07807. Positions 5-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 210204DHFRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 396Substrate bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0262.
GeneTreeiENSGT00390000010283.
HOGENOMiHOG000040235.
InParanoidiP07807.
KOiK00287.
OMAiEMKYFRQ.
OrthoDBiEOG7Q8D07.

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.

P07807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGKIPIVG IVACLQPEMG IGFRGGLPWR LPSEMKYFRQ VTSLTKDPNK
60 70 80 90 100
KNALIMGRKT WESIPPKFRP LPNRMNVIIS RSFKDDFVHD KERSIVQSNS
110 120 130 140 150
LANAIMNLES NFKEHLERIY VIGGGEVYSQ IFSITDHWLI TKINPLDKNA
160 170 180 190 200
TPAMDTFLDA KKLEEVFSEQ DPAQLKEFLP PKVELPETDC DQRYSLEEKG
210
YCFEFTLYNR K
Length:211
Mass (Da):24,261
Last modified:July 4, 2005 - v2
Checksum:iE030CDE7DA481D5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271L → V in CAA68779 (PubMed:2827121).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00887 Genomic DNA. Translation: CAA68779.1.
M18578 Genomic DNA. Translation: AAB59331.1.
M26668 Genomic DNA. Translation: AAA34564.1.
Z75144 Genomic DNA. Translation: CAA99456.1.
BK006948 Genomic DNA. Translation: DAA11005.1.
PIRiJT0269. RDBYD.
RefSeqiNP_014879.1. NM_001183655.1.

Genome annotation databases

EnsemblFungiiYOR236W; YOR236W; YOR236W.
GeneIDi854411.
KEGGisce:YOR236W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00887 Genomic DNA. Translation: CAA68779.1.
M18578 Genomic DNA. Translation: AAB59331.1.
M26668 Genomic DNA. Translation: AAA34564.1.
Z75144 Genomic DNA. Translation: CAA99456.1.
BK006948 Genomic DNA. Translation: DAA11005.1.
PIRiJT0269. RDBYD.
RefSeqiNP_014879.1. NM_001183655.1.

3D structure databases

ProteinModelPortaliP07807.
SMRiP07807. Positions 5-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34628. 45 interactions.
DIPiDIP-4120N.
IntActiP07807. 4 interactions.
MINTiMINT-532257.
STRINGi4932.YOR236W.

Chemistry

BindingDBiP07807.
ChEMBLiCHEMBL2576.

Proteomic databases

MaxQBiP07807.
PaxDbiP07807.
PRIDEiP07807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR236W; YOR236W; YOR236W.
GeneIDi854411.
KEGGisce:YOR236W.

Organism-specific databases

CYGDiYOR236w.
SGDiS000005762. DFR1.

Phylogenomic databases

eggNOGiCOG0262.
GeneTreeiENSGT00390000010283.
HOGENOMiHOG000040235.
InParanoidiP07807.
KOiK00287.
OMAiEMKYFRQ.
OrthoDBiEOG7Q8D07.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BioCyciYEAST:YOR236W-MONOMER.
ReactomeiREACT_303865. E2F mediated regulation of DNA replication.
REACT_324954. Metabolism of folate and pterines.
REACT_342867. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_345909. G1/S-Specific Transcription.

Miscellaneous databases

NextBioi976601.
PROiP07807.

Gene expression databases

GenevestigatoriP07807.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the Saccharomyces cerevisiae dihydrofolate reductase gene (DFR1)."
    Lagosky P.A., Taylor G.R., Haynes R.H.
    Nucleic Acids Res. 15:10355-10371(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the dihydrofolate reductase gene of Saccharomyces cerevisiae."
    Fling M.E., Kopf J., Richards C.A.
    Gene 63:165-174(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Mapping and sequencing of the dihydrofolate reductase gene (DFR1) of Saccharomyces cerevisiae."
    Barclay B.J., Huang T., Nagel M.G., Misener V.L., Game J.C., Wahl G.M.
    Gene 63:175-185(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae."
    Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.
    Yeast 12:1575-1586(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDYR_YEAST
AccessioniPrimary (citable) accession number: P07807
Secondary accession number(s): D6W2T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1988
Last sequence update: July 4, 2005
Last modified: March 31, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1080 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.