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O62583 (DYR_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-1
Ordered Locus Names:ECU01_0170
AND
Name:DHFR-2
Ordered Locus Names:ECU01_1450
AND
Name:DHFR-3
Ordered Locus Names:ECU08_0080
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 – 205205Dihydrofolate reductase
PRO_0000186373

Regions

Domain1 – 201201DHFR
Nucleotide binding13 – 197NADP By similarity
Nucleotide binding62 – 643NADP By similarity
Nucleotide binding84 – 863NADP By similarity
Nucleotide binding118 – 1258NADP By similarity
Region29 – 346Substrate binding By similarity

Sites

Binding site71NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site781Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O62583 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 45450EAA534487DD

FASTA20522,883
        10         20         30         40         50         60 
MLALVVALAS HRGIGNANAL PWPRPLAADM AWFRTLSQSI PLISPDRIAL APSASNAVVM 

        70         80         90        100        110        120 
GRRTWDSIPS RFRPLANRIN VVLSRGPARS TENTFFIQTF EALDSLPLPP SSMTFVIGGR 

       130        140        150        160        170        180 
DVYSLALESG RPHLIFATEV FESPECDVFF PHIDWASYEK RDITRDVSRL IDRTLASAFY 

       190        200 
SPETATFTEN GTSFKMFLYT KPETR 

« Hide

References

« Hide 'large scale' references
[1]"First report on the systematic sequencing of the small genome of Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3 kbp region on chromosome I."
Duffieux F., Peyret P., Roe B.A., Vivares C.P.
Microb. Comp. Genomics 3:1-11(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence and analysis of chromosome I of the amitochondriate intracellular parasite Encephalitozoon cuniculi (Microspora)."
Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., Weissenbach J., Saurin W., Vivares C.P.
Genome Res. 11:198-207(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.
[3]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005644 Genomic DNA. Translation: CAA06647.1.
AL391737 Genomic DNA. Translation: CAD24887.1.
AL391737 Genomic DNA. Translation: CAD25017.1.
AL590448 Genomic DNA. Translation: CAD26313.1.
RefSeqNP_597137.1. NM_001041746.1.
XP_965852.1. XM_960759.1.
XP_965982.1. XM_960889.1.

3D structure databases

ProteinModelPortalO62583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6035.ECU08_0080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID859559.
860188.
860189.
KEGGecu:ECU01_0170.
ecu:ECU01_1450.
ecu:ECU08_0080.

Phylogenomic databases

eggNOGCOG0262.
HOGENOMHOG000040235.
KOK00287.
OMAPARSTEN.
OrthoDBEOG7Q8D07.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDYR_ENCCU
AccessionPrimary (citable) accession number: O62583
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 87 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways