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Protein

Dihydrofolate reductase

Gene

DFR1

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: -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: 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)DescriptionActionsGraphical viewLength
Binding sitei11NADP; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei72SubstrateBy similarity1
Binding sitei112Substrate; via carbonyl oxygen1 Publication1
Binding sitei118Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 24NADP1 Publication7
Nucleotide bindingi56 – 58NADP1 Publication3
Nucleotide bindingi78 – 80NADP1 Publication3
Nucleotide bindingi113 – 120NADP1 Publication8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processOne-carbon metabolism
LigandNADP

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2329
DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863741 – 192Dihydrofolate reductaseAdd BLAST192

Proteomic databases

PRIDEiP22906

Interactioni

Chemistry databases

BindingDBiP22906

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Turni14 – 17Combined sources4
Beta strandi18 – 21Combined sources4
Helixi30 – 41Combined sources12
Beta strandi44 – 47Combined sources4
Beta strandi49 – 55Combined sources7
Helixi56 – 61Combined sources6
Helixi64 – 66Combined sources3
Beta strandi72 – 77Combined sources6
Beta strandi79 – 81Combined sources3
Beta strandi84 – 87Combined sources4
Beta strandi90 – 95Combined sources6
Helixi96 – 101Combined sources6
Beta strandi105 – 111Combined sources7
Helixi115 – 121Combined sources7
Beta strandi127 – 136Combined sources10
Helixi140 – 142Combined sources3
Helixi153 – 155Combined sources3
Beta strandi156 – 158Combined sources3
Helixi161 – 168Combined sources8
Beta strandi175 – 179Combined sources5
Beta strandi182 – 191Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22906

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 191DHFRPROSITE-ProRule annotationAdd BLAST187

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 37Substrate binding1 Publication6

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated

Family and domain databases

CDDicd00209 DHFR, 1 hit
Gene3Di3.40.430.10, 1 hit
InterProiView protein in InterPro
IPR024072 DHFR-like_dom_sf
IPR017925 DHFR_CS
IPR001796 DHFR_dom
PfamiView protein in Pfam
PF00186 DHFR_1, 1 hit
SUPFAMiSSF53597 SSF53597, 1 hit
PROSITEiView protein in PROSITE
PS00075 DHFR_1, 1 hit
PS51330 DHFR_2, 1 hit

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)DescriptionActionsGraphical viewLength
Natural varianti2S → L in strain: SYNTEX CA755. 1
Natural varianti84K → E in strain: SYNTEX CA755. 1

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiDYR_CANAX
AccessioniPrimary (citable) accession number: P22906
Secondary accession number(s): O59840
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 110 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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