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P00378

- DYR_CHICK

UniProt

P00378 - DYR_CHICK

Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. May bind to mRNA.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91NADP; via amide nitrogen and carbonyl oxygen
    Binding sitei70 – 701Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 217NADP
    Nucleotide bindingi54 – 563NADP
    Nucleotide bindingi76 – 783NADP
    Nucleotide bindingi116 – 1238NADP

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: UniProtKB
    2. drug binding Source: UniProtKB
    3. mRNA binding Source: UniProtKB
    4. 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. response to methotrexate Source: UniProtKB-KW
    5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
    6. tetrahydrofolate metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Methotrexate resistance, One-carbon metabolism

    Keywords - Ligandi

    NADP, RNA-binding

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Gene namesi
    Name:DHFR
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 189189Dihydrofolate reductasePRO_0000186367Add
    BLAST

    Proteomic databases

    PaxDbiP00378.

    Interactioni

    Structurei

    Secondary structure

    1
    189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Beta strandi15 – 184
    Beta strandi23 – 253
    Helixi28 – 3912
    Beta strandi47 – 537
    Helixi54 – 596
    Helixi62 – 643
    Beta strandi70 – 756
    Beta strandi87 – 926
    Helixi93 – 1019
    Helixi103 – 1064
    Beta strandi109 – 1146
    Helixi118 – 1269
    Beta strandi127 – 14014
    Beta strandi145 – 1473
    Turni153 – 1553
    Beta strandi156 – 1583
    Beta strandi170 – 1723
    Beta strandi175 – 18410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DR1X-ray2.20A1-189[»]
    1DR2X-ray2.30A1-189[»]
    1DR3X-ray2.30A1-189[»]
    1DR4X-ray2.40A1-189[»]
    1DR5X-ray2.40A1-189[»]
    1DR6X-ray2.40A1-189[»]
    1DR7X-ray2.40A1-189[»]
    8DFRX-ray1.70A1-189[»]
    ProteinModelPortaliP00378.
    SMRiP00378. Positions 1-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00378.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 184182DHFRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 356Substrate binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0262.
    HOVERGENiHBG000773.
    InParanoidiP00378.

    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.

    P00378-1 [UniParc]FASTAAdd to Basket

    « Hide

    VRSLNSIVAV CQNMGIGKDG NLPWPPLRNE YKYFQRMTST SHVEGKQNAV    50
    IMGKKTWFSI PEKNRPLKDR INIVLSRELK EAPKGAHYLS KSLDDALALL 100
    DSPELKSKVD MVWIVGGTAV YKAAMEKPIN HRLFVTRILH EFESDTFFPE 150
    IDYKDFKLLT EYPGVPADIQ EEDGIQYKFE VYQKSVLAQ 189
    Length:189
    Mass (Da):21,650
    Last modified:July 21, 1986 - v1
    Checksum:iBC5F50C94BCA3EDA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411E → Q AA sequence (PubMed:8670138)Curated

    Sequence databases

    PIRiA00390. RDCHD.
    UniGeneiGga.2883.
    Gga.48831.

    Cross-referencesi

    Sequence databases

    PIRi A00390. RDCHD.
    UniGenei Gga.2883.
    Gga.48831.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DR1 X-ray 2.20 A 1-189 [» ]
    1DR2 X-ray 2.30 A 1-189 [» ]
    1DR3 X-ray 2.30 A 1-189 [» ]
    1DR4 X-ray 2.40 A 1-189 [» ]
    1DR5 X-ray 2.40 A 1-189 [» ]
    1DR6 X-ray 2.40 A 1-189 [» ]
    1DR7 X-ray 2.40 A 1-189 [» ]
    8DFR X-ray 1.70 A 1-189 [» ]
    ProteinModelPortali P00378.
    SMRi P00378. Positions 1-186.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00378.
    ChEMBLi CHEMBL2575.

    Proteomic databases

    PaxDbi P00378.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0262.
    HOVERGENi HBG000773.
    InParanoidi P00378.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    Miscellaneous databases

    EvolutionaryTracei P00378.
    PROi P00378.

    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. "Primary structure of chicken liver dihydrofolate reductase."
      Kumar A.A., Blankenship D.T., Kaufman B.T., Freisheim J.H.
      Biochemistry 19:667-678(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site."
      Fan Y.X., Ju M., Zhou J.M., Tsou C.L.
      Biochem. J. 315:97-102(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-22; 138-141 AND 158-161.
    3. "Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin."
      McTigue M.A., Davies J.F. II, Kaufman B.T., Kraut J.
      Biochemistry 31:7264-7273(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH NADPH AND DIHYDROBIOPTERIN.

    Entry informationi

    Entry nameiDYR_CHICK
    AccessioniPrimary (citable) accession number: P00378
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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