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)

P13955

- DYRA_STAAU

UniProt

P13955 - DYRA_STAAU

Protein

Dihydrofolate reductase type 1 from Tn4003

Gene

dfrA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei28 – 281Substrate
    Binding sitei58 – 581Substrate
    Binding sitei112 – 1121Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 82NADP1 Publication
    Nucleotide bindingi15 – 206NADP1 Publication
    Nucleotide bindingi44 – 474NADP1 Publication
    Nucleotide bindingi63 – 664NADP1 Publication
    Nucleotide bindingi93 – 986NADP1 Publication

    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 from Tn4003 (EC:1.5.1.3)
    Gene namesi
    Name:dfrA
    Encoded oniPlasmid pSK10 Publication
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441A → G: Increases trimethoprim sensitivity; when associated with F-99. 1 Publication
    Mutagenesisi99 – 991Y → F: Increases trimethoprim sensitivity; when associated with G-44. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 161160Dihydrofolate reductase type 1 from Tn4003PRO_0000186405Add
    BLAST

    Proteomic databases

    PRIDEiP13955.

    Structurei

    Secondary structure

    1
    161
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Beta strandi14 – 174
    Helixi26 – 3611
    Beta strandi39 – 446
    Helixi45 – 517
    Beta strandi58 – 636
    Beta strandi75 – 773
    Helixi81 – 844
    Beta strandi90 – 945
    Helixi96 – 1027
    Turni103 – 1053
    Beta strandi107 – 11610
    Beta strandi120 – 1234
    Turni129 – 1313
    Beta strandi132 – 1398
    Beta strandi143 – 1453
    Beta strandi150 – 1578

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W9SX-ray1.80A/B/C/D/E/F1-161[»]
    2W9TX-ray2.35A/B1-161[»]
    ProteinModelPortaliP13955.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13955.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 157156DHFRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 83Substrate binding

    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]
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13955-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLSIIVAHD KQRVIGYQNQ LPWHLPNDLK HIKQLTTGNT LVMARKTFNS    50
    IGKPLPNRRN VVLTNQASFH HEGVDVINSL DEIKELSGHV FIFGGQTLYE 100
    AMIDQVDDMY ITVIDGKFQG DTFFPPYTFE NWEVESSVEG QLDEKNTIPH 150
    TFLHLVRRKG K 161
    Length:161
    Mass (Da):18,461
    Last modified:January 23, 2007 - v3
    Checksum:iF829D6109A3AF3A0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13290 Genomic DNA. Translation: CAA31649.1.
    Y07536 Genomic DNA. Translation: CAA68824.1.
    PIRiS04164.
    RefSeqiNP_877983.1. NC_005054.1.
    YP_002790943.1. NC_012547.1.
    YP_003813115.1. NC_014369.1.
    YP_006937652.1. NC_013320.1.
    YP_006937707.1. NC_013321.1.
    YP_006938354.1. NC_013338.1.
    YP_006938562.1. NC_013343.1.

    Genome annotation databases

    GeneIDi13874802.
    13874858.
    13875495.
    13875735.
    2598376.
    7751508.
    9487075.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13290 Genomic DNA. Translation: CAA31649.1 .
    Y07536 Genomic DNA. Translation: CAA68824.1 .
    PIRi S04164.
    RefSeqi NP_877983.1. NC_005054.1.
    YP_002790943.1. NC_012547.1.
    YP_003813115.1. NC_014369.1.
    YP_006937652.1. NC_013320.1.
    YP_006937707.1. NC_013321.1.
    YP_006938354.1. NC_013338.1.
    YP_006938562.1. NC_013343.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W9S X-ray 1.80 A/B/C/D/E/F 1-161 [» ]
    2W9T X-ray 2.35 A/B 1-161 [» ]
    ProteinModelPortali P13955.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P13955.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13874802.
    13874858.
    13875495.
    13875735.
    2598376.
    7751508.
    9487075.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    Miscellaneous databases

    EvolutionaryTracei P13955.

    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. "Trimethoprim resistance transposon Tn4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS257."
      Rouch D.A., Messeroti L.J., Loo L.S.L., Jackson C.A., Skurray R.A.
      Mol. Microbiol. 3:161-175(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Transposon: Tn4003.
    2. "Identical genes for trimethoprim-resistant dihydrofolate reductase from Staphylococcus aureus in Australia and central Europe."
      Burdeska A., Ott M., Bannwarth W., Then R.L.
      FEBS Lett. 266:159-162(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 157/4696.
    3. "Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim."
      Heaslet H., Harris M., Fahnoe K., Sarver R., Putz H., Chang J., Subramanyam C., Barreiro G., Miller J.R.
      Proteins 76:706-717(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADPH AND TRIMETHOPRIM, MUTAGENESIS OF ALA-44 AND TYR-99.

    Entry informationi

    Entry nameiDYRA_STAAU
    AccessioniPrimary (citable) accession number: P13955
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two DhfR isozymes in S.aureus, this one is plasmid-encoded and is resistant to trimethoprim.

    Keywords - Technical termi

    3D-structure, Plasmid

    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