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P00384

- DYR22_ECOLX

UniProt

P00384 - DYR22_ECOLX

Protein

Dihydrofolate reductase type 2

Gene
N/A
Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. Functioni

    Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei32 – 321NADPBy similarity
    Binding sitei68 – 681Substrate; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi66 – 694NADPBy similarity

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. one-carbon metabolic process Source: UniProtKB-KW
    2. response to antibiotic Source: UniProtKB-KW
    3. response to drug Source: InterPro
    4. response to methotrexate Source: UniProtKB-KW
    5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic resistance, Methotrexate resistance, One-carbon metabolism, Trimethoprim resistance

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase type 2 (EC:1.5.1.3)
    Alternative name(s):
    Dihydrofolate reductase type II
    Encoded oniPlasmid IncW R3880 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7878Dihydrofolate reductase type 2PRO_0000186436Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP00384.
    SMRiP00384. Positions 19-77.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The active site is situated at the inner surface of a pore formed by the four subunits.By similarity

    Family and domain databases

    InterProiIPR009159. Dhfr_type_II.
    IPR008990. Elect_transpt_acc-like_dom.
    [Graphical view]
    PfamiPF06442. DHFR_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000199. Dhfr_type_II. 1 hit.
    SUPFAMiSSF50090. SSF50090. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P00384-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQSSDEANA PVAGQFALPL SATFGLGDRV RKKSGAAWQG QVVGWYCTKL   50
    TPEGYAVESE SHPGSVQIYP VAALERVA 78
    Length:78
    Mass (Da):8,195
    Last modified:July 21, 1986 - v1
    Checksum:iEE9B686CBE5BCB93
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00252 Genomic DNA. Translation: CAA23503.1.
    J01773 Genomic DNA. Translation: AAA72145.1.
    PIRiA00398. RDECD8.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00252 Genomic DNA. Translation: CAA23503.1 .
    J01773 Genomic DNA. Translation: AAA72145.1 .
    PIRi A00398. RDECD8.

    3D structure databases

    ProteinModelPortali P00384.
    SMRi P00384. Positions 19-77.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    Family and domain databases

    InterProi IPR009159. Dhfr_type_II.
    IPR008990. Elect_transpt_acc-like_dom.
    [Graphical view ]
    Pfami PF06442. DHFR_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000199. Dhfr_type_II. 1 hit.
    SUPFAMi SSF50090. SSF50090. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a R plasmid-associated, trimethoprim-resistant dihydrofolate reductase and determination of the nucleotide sequence of the reductase gene."
      Zolg J.W., Haenggi U.J.
      Nucleic Acids Res. 9:697-710(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence of a plasmid-encoded dihydrofolate reductase."
      Swift G., McCarthy B.J., Heffron F.
      Mol. Gen. Genet. 181:441-447(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiDYR22_ECOLX
    AccessioniPrimary (citable) accession number: P00384
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Type II plasmid-specified enzyme is practically insensitive to trimethoprim and methotrexate.

    Keywords - Technical termi

    Plasmid

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways

    External Data

    Dasty 3