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P22906

- DYR_CANAX

UniProt

P22906 - DYR_CANAX

Protein

Dihydrofolate reductase

Gene

DFR1

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 4 (01 Nov 1995)
      Previous versions | rss
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    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

    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.
    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

    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: October 1, 2014
    This is version 96 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