Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0ABQ4

- DYR_ECOLI

UniProt

P0ABQ4 - DYR_ECOLI

Protein

Dihydrofolate reductase

Gene

folA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 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.

    Catalytic activityi

    5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.1 PublicationPROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei5 – 51Substrate; via carbonyl oxygen
    Binding sitei7 – 71NADP; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei27 – 271Substrate
    Binding sitei52 – 521Substrate
    Binding sitei57 – 571Substrate
    Binding sitei76 – 761NADP; via carbonyl oxygen1 Publication
    Binding sitei113 – 1131Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 197NADP1 Publication
    Nucleotide bindingi45 – 462NADP1 Publication
    Nucleotide bindingi63 – 642NADP1 Publication
    Nucleotide bindingi95 – 1028NADP1 Publication

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: EcoCyc
    2. NADP binding Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. 10-formyltetrahydrofolate biosynthetic process Source: EcoCyc
    2. folic acid biosynthetic process Source: EcoCyc
    3. glycine biosynthetic process Source: InterPro
    4. nucleotide biosynthetic process Source: InterPro
    5. one-carbon metabolic process Source: UniProtKB-KW
    6. response to antibiotic Source: UniProtKB-KW
    7. response to drug Source: EcoliWiki
    8. response to methotrexate Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:DIHYDROFOLATEREDUCT-MONOMER.
    ECOL316407:JW0047-MONOMER.
    MetaCyc:DIHYDROFOLATEREDUCT-MONOMER.
    SABIO-RKP0ABQ4.
    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Gene namesi
    Name:folA
    Synonyms:tmrA
    Ordered Locus Names:b0048, JW0047
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10326. folA.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161M → F or S: Increases catalytic rate about 2-fold. 1 Publication
    Mutagenesisi16 – 161M → N: Increases catalytic rate about 2-fold. Increases catalytic rate about 7-fold; when associated with L-20; Y-42; F-92; A-85 and S-152. 1 Publication
    Mutagenesisi20 – 201M → I or V: Increases catalytic rate 2-fold. 1 Publication
    Mutagenesisi20 – 201M → L: Increases catalytic rate 2.5-fold. Increases catalytic rate about 7-fold; when associated with N-16; Y-42; F-92; A-85 and S-152. 1 Publication
    Mutagenesisi42 – 421M → V: Increases catalytic rate almost 2-fold. 1 Publication
    Mutagenesisi42 – 421M → Y: Increases catalytic rate almost 2-fold. Increases catalytic rate about 7-fold; when associated with N-16; L-20; A-85; F-92 and S-152. 1 Publication
    Mutagenesisi85 – 851C → A: Decreases catalytic rate by one third. Increases catalytic rate about 7-fold; when associated with N-16; L-20; Y-42; F-92 and S-152. 1 Publication
    Mutagenesisi92 – 921M → F: No effect. Increases catalytic rate about 7-fold; when associated with N-16; L-20; Y-42; A-85 and S-152. 1 Publication
    Mutagenesisi92 – 921M → L: No effect. 1 Publication
    Mutagenesisi152 – 1521C → S: Increases catalytic rate 1.5-fold. Increases catalytic rate about 7-fold; when associated with N-16; L-20; Y-42; A-85 and F-92. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 159159Dihydrofolate reductasePRO_0000186387Add
    BLAST

    Proteomic databases

    PaxDbiP0ABQ4.
    PRIDEiP0ABQ4.

    2D gel databases

    SWISS-2DPAGEP0ABQ4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABQ4.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    flxAP776094EBI-550404,EBI-553024

    Protein-protein interaction databases

    DIPiDIP-35824N.
    IntActiP0ABQ4. 16 interactions.
    MINTiMINT-1239602.
    STRINGi511145.b0048.

    Structurei

    Secondary structure

    1
    159
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98
    Helixi10 – 123
    Beta strandi13 – 164
    Turni17 – 193
    Helixi25 – 3511
    Beta strandi40 – 434
    Helixi44 – 507
    Beta strandi55 – 573
    Beta strandi59 – 624
    Beta strandi72 – 776
    Helixi78 – 858
    Beta strandi91 – 933
    Helixi97 – 1037
    Helixi104 – 1063
    Beta strandi108 – 1158
    Beta strandi122 – 1243
    Helixi130 – 1323
    Beta strandi133 – 1419
    Beta strandi147 – 1493
    Beta strandi151 – 1588

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DDRX-ray2.45A/B1-159[»]
    1DDSX-ray2.20A/B1-159[»]
    1DHIX-ray1.90A/B1-159[»]
    1DHJX-ray1.80A/B1-159[»]
    1DRAX-ray1.90A/B1-159[»]
    1DRBX-ray1.96A/B1-159[»]
    1DREX-ray2.60A1-159[»]
    1DRHX-ray2.30A1-159[»]
    1DYHX-ray1.90A/B1-159[»]
    1DYIX-ray1.90A/B1-159[»]
    1DYJX-ray1.85A/B1-159[»]
    1JOLX-ray1.96A/B1-159[»]
    1JOMX-ray1.90A1-159[»]
    1RA1X-ray1.90A1-159[»]
    1RA2X-ray1.60A1-159[»]
    1RA3X-ray1.80A1-159[»]
    1RA8X-ray1.80A1-159[»]
    1RA9X-ray1.55A1-159[»]
    1RB2X-ray2.10A/B1-159[»]
    1RB3X-ray2.30A/B1-159[»]
    1RC4X-ray1.90A1-159[»]
    1RD7X-ray2.60A/B1-159[»]
    1RE7X-ray2.60A/B1-159[»]
    1RF7X-ray1.80A1-159[»]
    1RG7X-ray2.00A1-159[»]
    1RH3X-ray2.40A1-159[»]
    1RX1X-ray2.00A1-159[»]
    1RX2X-ray1.80A1-159[»]
    1RX3X-ray2.20A1-159[»]
    1RX4X-ray2.20A1-159[»]
    1RX5X-ray2.30A1-159[»]
    1RX6X-ray2.00A1-159[»]
    1RX7X-ray2.30A1-159[»]
    1RX8X-ray2.80A1-159[»]
    1RX9X-ray1.90A1-159[»]
    1TDRX-ray2.50A/B1-159[»]
    2ANOX-ray2.68A1-159[»]
    2ANQX-ray2.13A1-159[»]
    2D0KX-ray1.90A/B2-159[»]
    2DRCX-ray1.90A/B1-159[»]
    2INQneutron diffraction2.20A/B1-159[»]
    3DAUX-ray1.50A1-159[»]
    3DRCX-ray1.90A/B1-159[»]
    3K74X-ray1.95A1-159[»]
    3KFYX-ray2.08A1-159[»]
    3OCHX-ray1.79A/B1-159[»]
    3QL3X-ray1.80A1-159[»]
    3QYLX-ray1.79A1-159[»]
    3QYOX-ray2.09A1-159[»]
    3R33X-ray2.09A1-159[»]
    4DFRX-ray1.70A/B1-159[»]
    4EIGX-ray2.50A1-159[»]
    4EIZX-ray2.20A/B1-159[»]
    4EJ1X-ray1.75A/B1-159[»]
    4FHBX-ray2.80A1-159[»]
    4GH8X-ray1.85A/B1-158[»]
    4I13X-ray1.60A1-159[»]
    4I1NX-ray1.89A1-159[»]
    4KJJX-ray1.15A1-159[»]
    4KJKX-ray1.35A1-159[»]
    4KJLX-ray1.38A1-159[»]
    4NX6X-ray1.35A1-159[»]
    4NX7X-ray1.15A1-159[»]
    5DFRX-ray2.30A1-159[»]
    6DFRX-ray2.40A1-159[»]
    7DFRX-ray2.50A1-159[»]
    DisProtiDP00301.
    ProteinModelPortaliP0ABQ4.
    SMRiP0ABQ4. Positions 1-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABQ4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 158158DHFRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0262.
    HOGENOMiHOG000040233.
    KOiK00287.
    OMAiCITHVEA.
    OrthoDBiEOG6KT2V2.
    PhylomeDBiP0ABQ4.

    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]
    PIRSFiPIRSF000194. DHFR. 1 hit.
    PRINTSiPR00070. DHFR.
    SUPFAMiSSF53597. SSF53597. 1 hit.
    PROSITEiPS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ABQ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI    50
    GRPLPGRKNI ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY 100
    EQFLPKAQKL YLTHIDAEVE GDTHFPDYEP DDWESVFSEF HDADAQNSHS 150
    YCFEILERR 159
    Length:159
    Mass (Da):17,999
    Last modified:July 21, 1986 - v1
    Checksum:i6A03CDCD7F5F8562
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281L → R in strain: B[RT500] isozyme 2.
    Natural varianti30 – 301W → G in strain: 1810.
    Natural varianti154 – 1541E → K in strain: B[MB1428].
    Natural varianti154 – 1541E → Q in strain: 1810.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01609 Genomic DNA. Translation: AAA87976.1.
    X05108 Genomic DNA. Translation: CAA28755.1.
    U00096 Genomic DNA. Translation: AAC73159.1.
    AP009048 Genomic DNA. Translation: BAB96616.1.
    PIRiA93704. RDECD.
    RefSeqiNP_414590.1. NC_000913.3.
    YP_488354.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73159; AAC73159; b0048.
    BAB96616; BAB96616; BAB96616.
    GeneIDi12933205.
    944790.
    KEGGiecj:Y75_p0048.
    eco:b0048.
    PATRICi32115195. VBIEscCol129921_0049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01609 Genomic DNA. Translation: AAA87976.1 .
    X05108 Genomic DNA. Translation: CAA28755.1 .
    U00096 Genomic DNA. Translation: AAC73159.1 .
    AP009048 Genomic DNA. Translation: BAB96616.1 .
    PIRi A93704. RDECD.
    RefSeqi NP_414590.1. NC_000913.3.
    YP_488354.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DDR X-ray 2.45 A/B 1-159 [» ]
    1DDS X-ray 2.20 A/B 1-159 [» ]
    1DHI X-ray 1.90 A/B 1-159 [» ]
    1DHJ X-ray 1.80 A/B 1-159 [» ]
    1DRA X-ray 1.90 A/B 1-159 [» ]
    1DRB X-ray 1.96 A/B 1-159 [» ]
    1DRE X-ray 2.60 A 1-159 [» ]
    1DRH X-ray 2.30 A 1-159 [» ]
    1DYH X-ray 1.90 A/B 1-159 [» ]
    1DYI X-ray 1.90 A/B 1-159 [» ]
    1DYJ X-ray 1.85 A/B 1-159 [» ]
    1JOL X-ray 1.96 A/B 1-159 [» ]
    1JOM X-ray 1.90 A 1-159 [» ]
    1RA1 X-ray 1.90 A 1-159 [» ]
    1RA2 X-ray 1.60 A 1-159 [» ]
    1RA3 X-ray 1.80 A 1-159 [» ]
    1RA8 X-ray 1.80 A 1-159 [» ]
    1RA9 X-ray 1.55 A 1-159 [» ]
    1RB2 X-ray 2.10 A/B 1-159 [» ]
    1RB3 X-ray 2.30 A/B 1-159 [» ]
    1RC4 X-ray 1.90 A 1-159 [» ]
    1RD7 X-ray 2.60 A/B 1-159 [» ]
    1RE7 X-ray 2.60 A/B 1-159 [» ]
    1RF7 X-ray 1.80 A 1-159 [» ]
    1RG7 X-ray 2.00 A 1-159 [» ]
    1RH3 X-ray 2.40 A 1-159 [» ]
    1RX1 X-ray 2.00 A 1-159 [» ]
    1RX2 X-ray 1.80 A 1-159 [» ]
    1RX3 X-ray 2.20 A 1-159 [» ]
    1RX4 X-ray 2.20 A 1-159 [» ]
    1RX5 X-ray 2.30 A 1-159 [» ]
    1RX6 X-ray 2.00 A 1-159 [» ]
    1RX7 X-ray 2.30 A 1-159 [» ]
    1RX8 X-ray 2.80 A 1-159 [» ]
    1RX9 X-ray 1.90 A 1-159 [» ]
    1TDR X-ray 2.50 A/B 1-159 [» ]
    2ANO X-ray 2.68 A 1-159 [» ]
    2ANQ X-ray 2.13 A 1-159 [» ]
    2D0K X-ray 1.90 A/B 2-159 [» ]
    2DRC X-ray 1.90 A/B 1-159 [» ]
    2INQ neutron diffraction 2.20 A/B 1-159 [» ]
    3DAU X-ray 1.50 A 1-159 [» ]
    3DRC X-ray 1.90 A/B 1-159 [» ]
    3K74 X-ray 1.95 A 1-159 [» ]
    3KFY X-ray 2.08 A 1-159 [» ]
    3OCH X-ray 1.79 A/B 1-159 [» ]
    3QL3 X-ray 1.80 A 1-159 [» ]
    3QYL X-ray 1.79 A 1-159 [» ]
    3QYO X-ray 2.09 A 1-159 [» ]
    3R33 X-ray 2.09 A 1-159 [» ]
    4DFR X-ray 1.70 A/B 1-159 [» ]
    4EIG X-ray 2.50 A 1-159 [» ]
    4EIZ X-ray 2.20 A/B 1-159 [» ]
    4EJ1 X-ray 1.75 A/B 1-159 [» ]
    4FHB X-ray 2.80 A 1-159 [» ]
    4GH8 X-ray 1.85 A/B 1-158 [» ]
    4I13 X-ray 1.60 A 1-159 [» ]
    4I1N X-ray 1.89 A 1-159 [» ]
    4KJJ X-ray 1.15 A 1-159 [» ]
    4KJK X-ray 1.35 A 1-159 [» ]
    4KJL X-ray 1.38 A 1-159 [» ]
    4NX6 X-ray 1.35 A 1-159 [» ]
    4NX7 X-ray 1.15 A 1-159 [» ]
    5DFR X-ray 2.30 A 1-159 [» ]
    6DFR X-ray 2.40 A 1-159 [» ]
    7DFR X-ray 2.50 A 1-159 [» ]
    DisProti DP00301.
    ProteinModelPortali P0ABQ4.
    SMRi P0ABQ4. Positions 1-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35824N.
    IntActi P0ABQ4. 16 interactions.
    MINTi MINT-1239602.
    STRINGi 511145.b0048.

    Chemistry

    BindingDBi P0ABQ4.
    ChEMBLi CHEMBL1809.

    2D gel databases

    SWISS-2DPAGE P0ABQ4.

    Proteomic databases

    PaxDbi P0ABQ4.
    PRIDEi P0ABQ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73159 ; AAC73159 ; b0048 .
    BAB96616 ; BAB96616 ; BAB96616 .
    GeneIDi 12933205.
    944790.
    KEGGi ecj:Y75_p0048.
    eco:b0048.
    PATRICi 32115195. VBIEscCol129921_0049.

    Organism-specific databases

    EchoBASEi EB0322.
    EcoGenei EG10326. folA.

    Phylogenomic databases

    eggNOGi COG0262.
    HOGENOMi HOG000040233.
    KOi K00287.
    OMAi CITHVEA.
    OrthoDBi EOG6KT2V2.
    PhylomeDBi P0ABQ4.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    BioCyci EcoCyc:DIHYDROFOLATEREDUCT-MONOMER.
    ECOL316407:JW0047-MONOMER.
    MetaCyc:DIHYDROFOLATEREDUCT-MONOMER.
    SABIO-RK P0ABQ4.

    Miscellaneous databases

    EvolutionaryTracei P0ABQ4.
    PROi P0ABQ4.

    Gene expression databases

    Genevestigatori P0ABQ4.

    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 ]
    PIRSFi PIRSF000194. DHFR. 1 hit.
    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 amino-acid sequence of the dihydrofolate reductase of a trimethoprim-resistant strain of Escherichia coli."
      Stone D., Phillips A.W., Burchall J.J.
      Eur. J. Biochem. 72:613-624(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOZYME 1).
      Strain: B [RT500].
    2. "Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli."
      Bennett C.D., Rodkey J.A., Sondey J.M., Hirschmann R.
      Biochemistry 17:1328-1337(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: B [MB1428].
    3. "Nucleotide sequence of the E coli gene coding for dihydrofolate reductase."
      Smith D.R., Calvo J.M.
      Nucleic Acids Res. 8:2255-2274(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding."
      Baccanari D.P., Stone D., Kuyper L.
      J. Biol. Chem. 256:1738-1747(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOZYME 2).
      Strain: B [RT500].
    5. "Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim."
      Flensburg J., Skoeld O.
      Eur. J. Biochem. 162:473-476(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 1810.
    6. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    8. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7-A resolution. II. Environment of bound NADPH and implications for catalysis."
      Filman D.J., Bolin J.T., Matthews D.A., Kraut J.
      J. Biol. Chem. 257:13663-13672(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    11. "Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state."
      Bystroff C., Oatley S.J., Kraut J.
      Biochemistry 29:3263-3277(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    12. "Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding."
      Bystroff C., Kraut J.
      Biochemistry 30:2227-2239(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    13. "Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications."
      Reyes V.M., Sawaya M.R., Brown K.A., Kraut J.
      Biochemistry 34:2710-2723(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH NADPH; FOLATE; 5-DEAZAFOLATE AND 5,10-DIDEAZATETRAHYDROFOLATE.
    14. "Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4."
      Lee H., Reyes V.M., Kraut J.
      Biochemistry 35:7012-7020(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH 5-FORMYLTETRAHYDROFOLATE.
    15. "Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence."
      Sawaya M.R., Kraut J.
      Biochemistry 36:586-603(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH NADPH; METHOTREXATE AND TETRAHYDROFOLATE.
    16. "Evolutional design of a hyperactive cysteine- and methionine-free mutant of Escherichia coli dihydrofolate reductase."
      Iwakura M., Maki K., Takahashi H., Takenawa T., Yokota A., Katayanagi K., Kamiyama T., Gekko K.
      J. Biol. Chem. 281:13234-13246(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FOLATE, CATALYTIC ACTIVITY, MUTAGENESIS OF MET-16; MET-20; MET-42; CYS-85; MET-92 AND CYS-152, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "A 2.13 A structure of E. coli dihydrofolate reductase bound to a novel competitive inhibitor reveals a new binding surface involving the M20 loop region."
      Summerfield R.L., Daigle D.M., Mayer S., Mallik D., Hughes D.W., Jackson S.G., Sulek M., Organ M.G., Brown E.D., Junop M.S.
      J. Med. Chem. 49:6977-6986(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
    18. "Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate."
      Bennett B., Langan P., Coates L., Mustyakimov M., Schoenborn B., Howell E.E., Dealwis C.
      Proc. Natl. Acad. Sci. U.S.A. 103:18493-18498(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NEUTRON DIFFRACTION (2.20 ANGSTROMS) IN COMPLEX WITH METHOTREXATE.
    19. "X-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor design."
      Bennett B.C., Wan Q., Ahmad M.F., Langan P., Dealwis C.G.
      J. Struct. Biol. 166:162-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH METHOTREXATE AND NADPH.

    Entry informationi

    Entry nameiDYR_ECOLI
    AccessioniPrimary (citable) accession number: P0ABQ4
    Secondary accession number(s): P00379
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The strain K12 sequence is shown.
    Strain B [RT500] is resistant to 500 micrograms per milliliter of trimethoprim.
    Strain B [MB1428] is methotrexate-resistant.

    Keywords - Technical termi

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3