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P36591 (DYR_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. 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:dfr1
ORF Names:SPCC1223.08c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

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 – 461461Dihydrofolate reductase
PRO_0000186377

Regions

Domain233 – 447215DHFR
Nucleotide binding246 – 2527NADP By similarity
Nucleotide binding292 – 2943NADP By similarity
Nucleotide binding314 – 3163NADP By similarity
Nucleotide binding365 – 3728NADP By similarity
Region260 – 2656Substrate binding By similarity

Sites

Binding site2391NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site3081Substrate By similarity

Experimental info

Sequence conflict126 – 1272QP → HA in AAA57051. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36591 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: F6A3695F537A03C9

FASTA46151,523
        10         20         30         40         50         60 
MSKPLKVLCL HGWIQSGPVF SKKMGSVQKY LSKYAELHFP TGPVVADEEA DPNDEEEKKR 

        70         80         90        100        110        120 
LAALGGEQNG GKFGWFEVED FKNTYGSWDE SLECINQYMQ EKGPFDGLIG FSQGAGIGAM 

       130        140        150        160        170        180 
LAQMLQPGQP PNPYVQHPPF KFVVFVGGFR AEKPEFDHFY NPKLTTPSLH IAGTSDTLVP 

       190        200        210        220        230        240 
LARSKQLVER CENAHVLLHP GQHIVPQQAV YKTGIRDFMF SAPTKEPTKH PRDLTMIVAV 

       250        260        270        280        290        300 
SSPNLGIGKK NSMPWHIKQE MAYFANVTSS TESSGQLEEG KSKIMNVVIM GRSCYDSLPK 

       310        320        330        340        350        360 
KNRPLKDRIN IVITRNSNYN FGLTKKEKMP ENLYAADCID SALDLVAEKY GADSDIQVGK 

       370        380        390        400        410        420 
VFIIGGSFLY GSALYHPLTK NLLFTRIHKE YPCDSFFPFE PAESSDWVRK AHPELEKFVG 

       430        440        450        460 
IPVEEGRLKA ASSNKEEVEI EFELYGKNDD VNVALEKLSI C 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13703 mRNA. Translation: AAA57051.1.
CU329672 Genomic DNA. Translation: CAA20877.1.
PIRT43248.
RefSeqNP_588353.1. NM_001023344.2.

3D structure databases

ProteinModelPortalP36591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275621. 8 interactions.
MINTMINT-4688829.
STRING4896.SPCC1223.08c-1.

Proteomic databases

PaxDbP36591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1223.08c.1; SPCC1223.08c.1:pep; SPCC1223.08c.
GeneID2539048.
KEGGspo:SPCC1223.08c.

Organism-specific databases

PomBaseSPCC1223.08c.

Phylogenomic databases

eggNOGCOG0262.
KOK00287.
OrthoDBEOG7Q8D07.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR005645. Serine_hydrolase_FSH.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
PF03959. FSH1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800222.

Entry information

Entry nameDYR_SCHPO
AccessionPrimary (citable) accession number: P36591
Secondary accession number(s): O74408
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways