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P00382

- DYR1_ECOLX

UniProt

P00382 - DYR1_ECOLX

Protein

Dihydrofolate reductase type 1

Gene

dhfrI

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  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.PROSITE-ProRule annotation

    Pathwayi

    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. response to antibiotic Source: UniProtKB-KW
    5. response to methotrexate Source: UniProtKB-KW
    6. 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 1 (EC:1.5.1.3)
    Alternative name(s):
    Dihydrofolate reductase type I
    Trimethoprim resistance protein
    Gene namesi
    Name:dhfrI
    Encoded oniPlasmid IncI1 R4832 Publications
    Plasmid pLMO1501 Publication
    Plasmid pLMO2291 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 157157Dihydrofolate reductase type 1PRO_0000186420Add
    BLAST

    Proteomic databases

    PRIDEiP00382.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP00382.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 156155DHFRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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.

    P00382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLSLMVAIS KNGVIGNGPD IPWSAKGEQL LFKAITYNQW LLVGRKTFES    50
    MGALPNRKYA VVTRSSFTSD NENVLIFPSI KDALTNLKKI TDHVIVSGGG 100
    EIYKSLIDQV DTLHISTIDI EPEGDVYFPE IPSNFRPVFT QDFASNINYS 150
    YQIWQKG 157
    Length:157
    Mass (Da):17,575
    Last modified:July 21, 1986 - v1
    Checksum:i487F818A40E4991B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751L → V in plasmid pLMO229.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00926 Genomic DNA. Translation: CAA25445.1.
    X17477 Genomic DNA. Translation: CAA35509.1.
    X17478 Genomic DNA. Translation: CAA35512.1.
    PIRiS03651. RDECD7.
    RefSeqiNP_065309.1. NC_002525.1.
    YP_004422906.1. NC_015472.1.
    YP_190212.1. NC_006671.1.

    Genome annotation databases

    GeneIDi10549022.
    1238688.
    3244885.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00926 Genomic DNA. Translation: CAA25445.1 .
    X17477 Genomic DNA. Translation: CAA35509.1 .
    X17478 Genomic DNA. Translation: CAA35512.1 .
    PIRi S03651. RDECD7.
    RefSeqi NP_065309.1. NC_002525.1.
    YP_004422906.1. NC_015472.1.
    YP_190212.1. NC_006671.1.

    3D structure databases

    ProteinModelPortali P00382.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2627.

    Proteomic databases

    PRIDEi P00382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 10549022.
    1238688.
    3244885.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    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. "The nucleotide sequence of the trimethoprim-resistant dihydrofolate reductase gene harbored by Tn7."
      Fling M.E., Richards C.
      Nucleic Acids Res. 11:5147-5158(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Transposon: Tn7.
    2. "Expression of the plasmid-encoded type I dihydrofolate reductase gene in cultured mammalian cells: a novel selectable marker."
      Simonsen C.S., Walter M., Levinson A.D.
      Nucleic Acids Res. 16:2235-2246(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Plasmid: IncI1 R483
    3. "The dhfrI trimethoprim resistance gene of Tn7 can be found at specific sites in other genetic surroundings."
      Sundstroem L., Skoeld O.
      Antimicrob. Agents Chemother. 34:642-650(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Plasmid: pLMO150 pLMO229
    4. "R plasmid dihydrofolate reductase with a dimeric subunit structure."
      Novak P., Stone D., Burchall J.J.
      J. Biol. Chem. 258:10956-10959(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-34.
      Plasmid: IncI1 R483

    Entry informationi

    Entry nameiDYR1_ECOLX
    AccessioniPrimary (citable) accession number: P00382
    Secondary accession number(s): P13923
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Plasmid, Transposable element

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3