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)

Q54801

- DYR_STRPN

UniProt

Q54801 - DYR_STRPN

Protein

Dihydrofolate reductase

Gene

dhfR

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei30 – 301SubstrateBy similarity
    Binding sitei61 – 611SubstrateBy similarity
    Binding sitei83 – 831NADP; via amide nitrogenBy similarity
    Binding sitei119 – 1191SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 102NADPBy similarity
    Nucleotide bindingi17 – 226NADPBy similarity
    Nucleotide bindingi46 – 494NADPBy similarity
    Nucleotide bindingi66 – 694NADPBy similarity
    Nucleotide bindingi100 – 1056NADPBy similarity

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: UniProtKB-EC
    2. NADP binding Source: InterPro
    3. protein binding Source: IntAct

    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. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic resistance, One-carbon metabolism, Trimethoprim resistance

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciSPNE170187:GHGN-1577-MONOMER.
    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Gene namesi
    Name:dhfR
    Synonyms:dfr
    Ordered Locus Names:SP_1571
    OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
    Taxonomic identifieri170187 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000585: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 168168Dihydrofolate reductasePRO_0000186417Add
    BLAST

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SP_0371Q97SJ04EBI-6473264,EBI-6473258

    Protein-protein interaction databases

    IntActiQ54801. 1 interaction.
    STRINGi170187.SP_1571.

    Structurei

    Secondary structure

    1
    168
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi16 – 194
    Helixi28 – 3811
    Beta strandi41 – 466
    Helixi47 – 526
    Turni53 – 553
    Beta strandi62 – 665
    Beta strandi75 – 828
    Helixi83 – 919
    Beta strandi97 – 1015
    Helixi103 – 1097
    Helixi110 – 1123
    Beta strandi114 – 12310
    Beta strandi128 – 1303
    Helixi137 – 1393
    Beta strandi140 – 1489
    Beta strandi158 – 1658

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IX9X-ray1.95A/B1-168[»]
    ProteinModelPortaliQ54801.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ54801.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 165162DHFRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 103Substrate bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0262.
    HOGENOMiHOG000040233.
    KOiK00287.
    OMAiFKALTMG.
    OrthoDBiEOG6KT2V2.

    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.

    Q54801-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKKIVAIWA QDEEGVIGKE NRLPWHLPAE LQHFKETTLN HAILMGRVTF    50
    DGMGRRLLPK RETLILTRNP EEKIDGVATF QDVQSVLDWY QAQEKNLYII 100
    GGKQIFQAFE PYLDEVIVTH IHARVEGDTY FPEELDLSLF ETVSSKFYAK 150
    DEKNPYDFTI QYRKRKEV 168
    Length:168
    Mass (Da):19,703
    Last modified:September 26, 2001 - v2
    Checksum:i4C3887E290B6303E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141E → D in strain: 21.
    Natural varianti20 – 201E → D in strain: 21, 30 and 1/1.
    Natural varianti60 – 601K → Q in strain: 30, 56 and 1/1.
    Natural varianti65 – 651I → V in strain: 92.
    Natural varianti70 – 701P → S in strain: 21, 56 and 1/1.
    Natural varianti74 – 741I → L in strain: 21.
    Natural varianti77 – 782VA → AV in strain: 30.
    Natural varianti81 – 811Q → H in strain: 21, 56 and 1/1.
    Natural varianti91 – 911Q → H in strain: 21.
    Natural varianti92 – 921A → D in strain: ATCC 49619.
    Natural varianti94 – 941E → D in strain: 21.
    Natural varianti100 – 1001I → L in strain: 21, 30, 56 and 1/1.
    Natural varianti111 – 1111P → S in strain: 56 and 1/1.
    Natural varianti135 – 1351L → F in strain: 21, 30, 56 and 1/1.
    Natural varianti141 – 1411E → D in strain: 56.
    Natural varianti147 – 1493FYA → SYT in strain: 21.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74777 Genomic DNA. Translation: CAA99035.1.
    Z74778 Genomic DNA. Translation: CAA99036.1.
    Z84378 Genomic DNA. Translation: CAB06418.1.
    Z84379 Genomic DNA. Translation: CAB06419.1.
    Z84380 Genomic DNA. Translation: CAB06420.1.
    Z84381 Genomic DNA. Translation: CAB06421.1.
    AE005672 Genomic DNA. Translation: AAK75658.1.
    PIRiA95183.
    RefSeqiNP_346018.1. NC_003028.3.

    Genome annotation databases

    EnsemblBacteriaiAAK75658; AAK75658; SP_1571.
    GeneIDi931270.
    KEGGispn:SP_1571.
    PATRICi19707567. VBIStrPne105772_1626.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74777 Genomic DNA. Translation: CAA99035.1 .
    Z74778 Genomic DNA. Translation: CAA99036.1 .
    Z84378 Genomic DNA. Translation: CAB06418.1 .
    Z84379 Genomic DNA. Translation: CAB06419.1 .
    Z84380 Genomic DNA. Translation: CAB06420.1 .
    Z84381 Genomic DNA. Translation: CAB06421.1 .
    AE005672 Genomic DNA. Translation: AAK75658.1 .
    PIRi A95183.
    RefSeqi NP_346018.1. NC_003028.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IX9 X-ray 1.95 A/B 1-168 [» ]
    ProteinModelPortali Q54801.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q54801. 1 interaction.
    STRINGi 170187.SP_1571.

    Chemistry

    BindingDBi Q54801.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK75658 ; AAK75658 ; SP_1571 .
    GeneIDi 931270.
    KEGGi spn:SP_1571.
    PATRICi 19707567. VBIStrPne105772_1626.

    Phylogenomic databases

    eggNOGi COG0262.
    HOGENOMi HOG000040233.
    KOi K00287.
    OMAi FKALTMG.
    OrthoDBi EOG6KT2V2.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    BioCyci SPNE170187:GHGN-1577-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q54801.

    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. Caspers P.
      Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49619 / 262 / CIP 104340 / Serotype 19F and Trimethoprim resistant 1/1 Johannesburg 1993.
    2. "Mutations in the dihydrofolate reductase gene of trimethoprim-resistant isolates of Streptococcus pneumoniae."
      Adrian P.V., Klugman K.P.
      Antimicrob. Agents Chemother. 41:2406-2413(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 30, 56, 92 and Trimethoprim resistant 21.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-334 / TIGR4.

    Entry informationi

    Entry nameiDYR_STRPN
    AccessioniPrimary (citable) accession number: Q54801
    Secondary accession number(s): O08440
    , O08441, O08442, O08443, Q54973
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Strains 1/1, 21, 30, 56 and 92 are trimethoprim resistant.

    Keywords - Technical termi

    3D-structure, Complete 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