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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: 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

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2329.

PTM / Processingi

Molecule processing

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

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
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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)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.

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
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...

Chemistry databases

BindingDBiP22906.
ChEMBLiCHEMBL2329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Miscellaneous databases

EvolutionaryTraceiP22906.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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...

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 2, 2016
This is version 105 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

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 one 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.