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Protein

Dihydrofolate reductase

Gene

dfr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Pathway: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydrofolate reductase (dfr1)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei308 – 3081SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi246 – 2527NADPBy similarity
Nucleotide bindingi292 – 2943NADPBy similarity
Nucleotide bindingi314 – 3163NADPBy similarity
Nucleotide bindingi365 – 3728NADPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • dihydrofolate reductase activity Source: PomBase
  • NADP binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_306641. E2F mediated regulation of DNA replication.
REACT_332309. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_333030. Metabolism of folate and pterines.
REACT_343222. G1/S-Specific Transcription.
UniPathwayiUPA00077; UER00158.

Protein family/group databases

ESTHERischpo-dyr. FSH1.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:dfr1
ORF Names:SPCC1223.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1223.08c.
PomBaseiSPCC1223.08c. dfr1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Dihydrofolate reductasePRO_0000186377Add
BLAST

Proteomic databases

MaxQBiP36591.
PaxDbiP36591.

Interactioni

Protein-protein interaction databases

BioGridi275621. 4 interactions.
MINTiMINT-4688829.
STRINGi4896.SPCC1223.08c.1.

Structurei

3D structure databases

ProteinModelPortaliP36591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini233 – 447215DHFRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 2656Substrate bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0262.
InParanoidiP36591.
KOiK00287.
OrthoDBiEOG7Q8D07.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR005645. Serine_hydrolase_FSH.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
PF03959. FSH1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53474. SSF53474. 2 hits.
SSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPLKVLCL HGWIQSGPVF SKKMGSVQKY LSKYAELHFP TGPVVADEEA
60 70 80 90 100
DPNDEEEKKR LAALGGEQNG GKFGWFEVED FKNTYGSWDE SLECINQYMQ
110 120 130 140 150
EKGPFDGLIG FSQGAGIGAM LAQMLQPGQP PNPYVQHPPF KFVVFVGGFR
160 170 180 190 200
AEKPEFDHFY NPKLTTPSLH IAGTSDTLVP LARSKQLVER CENAHVLLHP
210 220 230 240 250
GQHIVPQQAV YKTGIRDFMF SAPTKEPTKH PRDLTMIVAV SSPNLGIGKK
260 270 280 290 300
NSMPWHIKQE MAYFANVTSS TESSGQLEEG KSKIMNVVIM GRSCYDSLPK
310 320 330 340 350
KNRPLKDRIN IVITRNSNYN FGLTKKEKMP ENLYAADCID SALDLVAEKY
360 370 380 390 400
GADSDIQVGK VFIIGGSFLY GSALYHPLTK NLLFTRIHKE YPCDSFFPFE
410 420 430 440 450
PAESSDWVRK AHPELEKFVG IPVEEGRLKA ASSNKEEVEI EFELYGKNDD
460
VNVALEKLSI C
Length:461
Mass (Da):51,523
Last modified:May 30, 2000 - v2
Checksum:iF6A3695F537A03C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1272QP → HA in AAA57051 (PubMed:8088538).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13703 mRNA. Translation: AAA57051.1.
CU329672 Genomic DNA. Translation: CAA20877.1.
PIRiT43248.
RefSeqiNP_588353.1. NM_001023344.2.

Genome annotation databases

EnsemblFungiiSPCC1223.08c.1; SPCC1223.08c.1:pep; SPCC1223.08c.
GeneIDi2539048.
KEGGispo:SPCC1223.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13703 mRNA. Translation: AAA57051.1.
CU329672 Genomic DNA. Translation: CAA20877.1.
PIRiT43248.
RefSeqiNP_588353.1. NM_001023344.2.

3D structure databases

ProteinModelPortaliP36591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275621. 4 interactions.
MINTiMINT-4688829.
STRINGi4896.SPCC1223.08c.1.

Protein family/group databases

ESTHERischpo-dyr. FSH1.

Proteomic databases

MaxQBiP36591.
PaxDbiP36591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1223.08c.1; SPCC1223.08c.1:pep; SPCC1223.08c.
GeneIDi2539048.
KEGGispo:SPCC1223.08c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1223.08c.
PomBaseiSPCC1223.08c. dfr1.

Phylogenomic databases

eggNOGiCOG0262.
InParanoidiP36591.
KOiK00287.
OrthoDBiEOG7Q8D07.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
ReactomeiREACT_306641. E2F mediated regulation of DNA replication.
REACT_332309. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_333030. Metabolism of folate and pterines.
REACT_343222. G1/S-Specific Transcription.

Miscellaneous databases

NextBioi20800222.
PROiP36591.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR005645. Serine_hydrolase_FSH.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
PF03959. FSH1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53474. SSF53474. 2 hits.
SSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The isolation and characterization of the gene (dfr1) encoding dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe."
    Bertani L.E., Campbell J.L.
    Gene 147:131-135(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiDYR_SCHPO
AccessioniPrimary (citable) accession number: P36591
Secondary accession number(s): O74408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: June 24, 2015
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.