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Protein

Dihydrofolate reductase

Gene

DFR1

Organism
Candida albicans (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.

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111NADP; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei72 – 721SubstrateBy similarity
Binding sitei112 – 1121Substrate; via carbonyl oxygen
Binding sitei118 – 1181Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 247NADP1 Publication
Nucleotide bindingi56 – 583NADP1 Publication
Nucleotide bindingi78 – 803NADP1 Publication
Nucleotide bindingi113 – 1208NADP1 Publication

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:DFR1
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Dihydrofolate reductasePRO_0000186374Add
BLAST

Interactioni

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Turni14 – 174Combined sources
Beta strandi18 – 214Combined sources
Helixi30 – 4112Combined sources
Beta strandi44 – 474Combined sources
Beta strandi49 – 557Combined sources
Helixi56 – 616Combined sources
Helixi64 – 663Combined sources
Beta strandi72 – 776Combined sources
Beta strandi79 – 813Combined sources
Beta strandi84 – 874Combined sources
Beta strandi90 – 956Combined sources
Helixi96 – 1016Combined sources
Beta strandi105 – 1117Combined sources
Helixi115 – 1217Combined sources
Beta strandi127 – 13610Combined sources
Helixi140 – 1423Combined sources
Helixi153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 1688Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi182 – 19110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AI9X-ray1.85A/B1-192[»]
1AOEX-ray1.60A/B1-192[»]
1IA1X-ray1.70A/B1-192[»]
1IA2X-ray1.82A/B1-192[»]
1IA3X-ray1.78A/B1-192[»]
1IA4X-ray1.85A/B1-192[»]
1M78X-ray1.71A/B1-192[»]
1M79X-ray1.70A/B1-192[»]
1M7AX-ray1.76A/B1-192[»]
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[»]
4HOEX-ray1.76A/B1-192[»]
4HOFX-ray1.76A/B1-192[»]
ProteinModelPortaliP22906.
SMRiP22906. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22906.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 191187DHFRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 376Substrate binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0262.

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.

P22906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPNVAIIV AALKPALGIG YKGKMPWRLR KEIRYFKDVT TRTTKPNTRN
60 70 80 90 100
AVIMGRKTWE SIPQKFRPLP DRLNIILSRS YENKIIDDNI IHASSIESSL
110 120 130 140 150
NLVSDVERVF IIGGAEIYNE LINNSLVSHL LITEIEHPSP ESIEMDTFLK
160 170 180 190
FPLESWTKQP KSELQKFVGD TVLEDDIKEG DFTYNYTLWT RK
Length:192
Mass (Da):22,139
Last modified:November 1, 1995 - v4
Checksum:iD8E3BEAC1DCADB4C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → L in strain: SYNTEX CA755.
Natural varianti84 – 841K → E in strain: SYNTEX CA755.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78968 Genomic DNA. Translation: CAA55561.1.
U84588 Genomic DNA. Translation: AAC05610.1.
PIRiA32203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78968 Genomic DNA. Translation: CAA55561.1.
U84588 Genomic DNA. Translation: AAC05610.1.
PIRiA32203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AI9X-ray1.85A/B1-192[»]
1AOEX-ray1.60A/B1-192[»]
1IA1X-ray1.70A/B1-192[»]
1IA2X-ray1.82A/B1-192[»]
1IA3X-ray1.78A/B1-192[»]
1IA4X-ray1.85A/B1-192[»]
1M78X-ray1.71A/B1-192[»]
1M79X-ray1.70A/B1-192[»]
1M7AX-ray1.76A/B1-192[»]
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[»]
4HOEX-ray1.76A/B1-192[»]
4HOFX-ray1.76A/B1-192[»]
ProteinModelPortaliP22906.
SMRiP22906. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP22906.
ChEMBLiCHEMBL2329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0262.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Miscellaneous databases

EvolutionaryTraceiP22906.

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

  1. "Sequence of a dihydrofolate reductase-encoding gene from Candida albicans."
    Daly S., Mastromei G., Yacoub A., Lorenzetti R.
    Gene 147:115-118(1993) [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(1988) [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(1996) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR.

Entry informationi

Entry nameiDYR_CANAX
AccessioniPrimary (citable) accession number: P22906
Secondary accession number(s): O59840
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 98 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.