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P22906

- DYR_CANAX

UniProt

P22906 - DYR_CANAX

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Protein

Dihydrofolate reductase

Gene
DFR1
Organism
Candida albicans (Yeast)
Status
Reviewed - 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.

Pathwayi

Sites

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

Regions

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

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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

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 – 138
Turni14 – 174
Beta strandi18 – 214
Helixi30 – 4112
Beta strandi44 – 474
Beta strandi49 – 557
Helixi56 – 616
Helixi64 – 663
Beta strandi72 – 776
Beta strandi79 – 813
Beta strandi84 – 874
Beta strandi90 – 956
Helixi96 – 1016
Beta strandi105 – 1117
Helixi115 – 1217
Beta strandi127 – 13610
Helixi140 – 1423
Helixi153 – 1553
Beta strandi156 – 1583
Helixi161 – 1688
Beta strandi175 – 1795
Beta strandi182 – 19110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP22906.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 191187DHFRAdd
BLAST

Region

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

Sequence similaritiesi

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

MSKPNVAIIV AALKPALGIG YKGKMPWRLR KEIRYFKDVT TRTTKPNTRN    50
AVIMGRKTWE SIPQKFRPLP DRLNIILSRS YENKIIDDNI IHASSIESSL 100
NLVSDVERVF IIGGAEIYNE LINNSLVSHL LITEIEHPSP ESIEMDTFLK 150
FPLESWTKQP KSELQKFVGD TVLEDDIKEG DFTYNYTLWT RK 192
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:
EMBL
GenBank
DDBJ
Links Updated
X78968 Genomic DNA. Translation: CAA55561.1.
U84588 Genomic DNA. Translation: AAC05610.1.
PIRiA32203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78968 Genomic DNA. Translation: CAA55561.1 .
U84588 Genomic DNA. Translation: AAC05610.1 .
PIRi A32203.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AI9 X-ray 1.85 A/B 1-192 [» ]
1AOE X-ray 1.60 A/B 1-192 [» ]
1IA1 X-ray 1.70 A/B 1-192 [» ]
1IA2 X-ray 1.82 A/B 1-192 [» ]
1IA3 X-ray 1.78 A/B 1-192 [» ]
1IA4 X-ray 1.85 A/B 1-192 [» ]
1M78 X-ray 1.71 A/B 1-192 [» ]
1M79 X-ray 1.70 A/B 1-192 [» ]
1M7A X-ray 1.76 A/B 1-192 [» ]
3QLR X-ray 2.15 A/B 3-192 [» ]
3QLS X-ray 1.73 A/B 3-192 [» ]
3QLW X-ray 2.50 A/B 3-192 [» ]
4H95 X-ray 2.60 A/B 4-192 [» ]
4H96 X-ray 2.60 A/B 4-192 [» ]
4H97 X-ray 2.20 A/B 3-192 [» ]
4HOE X-ray 1.76 A/B 1-192 [» ]
4HOF X-ray 1.76 A/B 1-192 [» ]
ProteinModelPortali P22906.
SMRi P22906. Positions 1-192.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P22906.
ChEMBLi CHEMBL2329.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0262.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Miscellaneous databases

EvolutionaryTracei P22906.

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: July 9, 2014
This is version 95 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

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