Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P22906 (DYR_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 93. 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
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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 – 192192Dihydrofolate reductase
PRO_0000186374

Regions

Domain5 – 191187DHFR
Nucleotide binding18 – 247NADP
Nucleotide binding56 – 583NADP
Nucleotide binding78 – 803NADP
Nucleotide binding113 – 1208NADP
Region32 – 376Substrate binding

Sites

Binding site111NADP; via amide nitrogen and carbonyl oxygen
Binding site721Substrate By similarity
Binding site1121Substrate; via carbonyl oxygen
Binding site1181Substrate

Natural variations

Natural variant21S → L in strain: SYNTEX CA755.
Natural variant841K → E in strain: SYNTEX CA755.

Secondary structure

........................................ 192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22906 [UniParc].

Last modified November 1, 1995. Version 4.
Checksum: D8E3BEAC1DCADB4C

FASTA19222,139
        10         20         30         40         50         60 
MSKPNVAIIV AALKPALGIG YKGKMPWRLR KEIRYFKDVT TRTTKPNTRN AVIMGRKTWE 

        70         80         90        100        110        120 
SIPQKFRPLP DRLNIILSRS YENKIIDDNI IHASSIESSL NLVSDVERVF IIGGAEIYNE 

       130        140        150        160        170        180 
LINNSLVSHL LITEIEHPSP ESIEMDTFLK FPLESWTKQP KSELQKFVGD TVLEDDIKEG 

       190 
DFTYNYTLWT RK 

« Hide

References

[1]"Sequence of a dihydrofolate reductase-encoding gene from Candida albicans."
Daly S., Mastromei G., Yacoub A., Lorenzetti R.
Gene 147:115-118(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 10127/5.
[2]"Characterization of Candida albicans dihydrofolate reductase."
Baccanari D.P., Tansik R.L., Joyner S.S., Fling M.E., Smith P.L., Freisheim J.H.
J. Biol. Chem. 264:1100-1107(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25, NUCLEOTIDE SEQUENCE OF 26-36.
[3]"X-ray crystallographic studies of Candida albicans dihydrofolate reductase. High resolution structures of the holoenzyme and an inhibited ternary complex."
Whitlow M., Howard A.J., Stewart D., Hardman K.D., Kuyper L.F., Baccanari D.P., Fling M.E., Tansik R.L.
J. Biol. Chem. 272:30289-30298(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
Strain: SYNTEX CA755.
[4]"X-Ray crystal structures of Candida albicans dihydrofolate reductase: high resolution ternary complexes in which the dihydronicotinamide moiety of NADPH is displaced by an inhibitor."
Whitlow M., Howard A.J., Stewart D., Hardman K.D., Chan J.H., Baccanari D.P., Tansik R.L., Hong J.S., Kuyper L.F.
J. Med. Chem. 44:2928-2932(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78968 Genomic DNA. Translation: CAA55561.1.
U84588 Genomic DNA. Translation: AAC05610.1.
PIRA32203.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AI9X-ray1.85A/B3-192[»]
1AOEX-ray1.60A/B3-192[»]
1IA1X-ray1.70A/B3-192[»]
1IA2X-ray1.82A/B3-192[»]
1IA3X-ray1.78A/B3-192[»]
1IA4X-ray1.85A/B3-192[»]
1M78X-ray1.71A/B3-192[»]
1M79X-ray1.70A/B3-192[»]
1M7AX-ray1.76A/B3-192[»]
3QLRX-ray2.15A/B3-192[»]
3QLSX-ray1.73A/B3-192[»]
3QLWX-ray2.50A/B3-192[»]
4H95X-ray2.60A/B4-192[»]
4H96X-ray2.60A/B4-192[»]
4H97X-ray2.20A/B3-192[»]
ProteinModelPortalP22906.
SMRP22906. Positions 1-192.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP22906.
ChEMBLCHEMBL2329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0262.

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.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22906.

Entry information

Entry nameDYR_CANAX
AccessionPrimary (citable) accession number: P22906
Secondary accession number(s): O59840
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: December 11, 2013
This is version 93 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways