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P0A017

- DYR_STAAU

UniProt

P0A017 - DYR_STAAU

Protein

Dihydrofolate reductase

Gene

folA

Organism
Staphylococcus aureus
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.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei28 – 281Substrate
    Binding sitei58 – 581Substrate
    Binding sitei101 – 1011NADP1 Publication
    Binding sitei112 – 1121Substrate
    Binding sitei122 – 1221NADP1 Publication

    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. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Short name:
    DHFR
    Gene namesi
    Name:folA
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 159158Dihydrofolate reductasePRO_0000186411Add
    BLAST

    Proteomic databases

    PRIDEiP0A017.

    Interactioni

    Structurei

    Secondary structure

    1
    159
    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
    Helixi80 – 856
    Beta strandi90 – 945
    Helixi96 – 1027
    Turni103 – 1053
    Beta strandi107 – 1148
    Beta strandi121 – 1233
    Turni129 – 1313
    Beta strandi132 – 1398
    Beta strandi150 – 1578

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W9GX-ray1.95A1-159[»]
    2W9HX-ray1.48A1-159[»]
    3FRAX-ray2.35X2-159[»]
    3FRBX-ray2.00X2-159[»]
    3FRDX-ray2.10X2-159[»]
    3FREX-ray2.20X2-159[»]
    3FRFX-ray2.20X2-159[»]
    3FY8X-ray2.20X2-159[»]
    3FY9X-ray2.25X2-159[»]
    3FYVX-ray2.20X2-159[»]
    3FYWX-ray2.10X2-159[»]
    3I8AX-ray2.41X2-158[»]
    3LG4X-ray3.15A/B1-158[»]
    3M08X-ray2.01A2-158[»]
    3M09X-ray2.01A2-158[»]
    3SGYX-ray2.60A/B2-158[»]
    3SH2X-ray3.00A/B2-158[»]
    3SQYX-ray1.50X1-159[»]
    3SR5X-ray1.68X2-159[»]
    3SRQX-ray1.69X1-159[»]
    3SRRX-ray1.70X1-159[»]
    3SRSX-ray1.70X1-159[»]
    3SRUX-ray1.70X1-159[»]
    3SRWX-ray1.70X1-159[»]
    4FGGX-ray2.30A1-159[»]
    4FGHX-ray2.50A1-159[»]
    4LAEX-ray1.69X1-159[»]
    4LAGX-ray1.70X1-159[»]
    4LAHX-ray1.88X1-159[»]
    4LEKX-ray1.70X1-159[»]
    ProteinModelPortaliP0A017.
    SMRiP0A017. Positions 2-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A017.

    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

    Phylogenomic databases

    eggNOGiCOG0262.

    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.

    P0A017-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES    50
    IGKPLPNRRN VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE 100
    EMIDKVDDMY ITVIEGKFRG DTFFPPYTFE DWEVASSVEG KLDEKNTIPH 150
    TFLHLIRKK 159
    Length:159
    Mass (Da):18,251
    Last modified:January 23, 2007 - v2
    Checksum:i811898409FEAFAAB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z16422 Genomic DNA. Translation: CAA78910.1.
    PIRiS32014.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z16422 Genomic DNA. Translation: CAA78910.1 .
    PIRi S32014.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W9G X-ray 1.95 A 1-159 [» ]
    2W9H X-ray 1.48 A 1-159 [» ]
    3FRA X-ray 2.35 X 2-159 [» ]
    3FRB X-ray 2.00 X 2-159 [» ]
    3FRD X-ray 2.10 X 2-159 [» ]
    3FRE X-ray 2.20 X 2-159 [» ]
    3FRF X-ray 2.20 X 2-159 [» ]
    3FY8 X-ray 2.20 X 2-159 [» ]
    3FY9 X-ray 2.25 X 2-159 [» ]
    3FYV X-ray 2.20 X 2-159 [» ]
    3FYW X-ray 2.10 X 2-159 [» ]
    3I8A X-ray 2.41 X 2-158 [» ]
    3LG4 X-ray 3.15 A/B 1-158 [» ]
    3M08 X-ray 2.01 A 2-158 [» ]
    3M09 X-ray 2.01 A 2-158 [» ]
    3SGY X-ray 2.60 A/B 2-158 [» ]
    3SH2 X-ray 3.00 A/B 2-158 [» ]
    3SQY X-ray 1.50 X 1-159 [» ]
    3SR5 X-ray 1.68 X 2-159 [» ]
    3SRQ X-ray 1.69 X 1-159 [» ]
    3SRR X-ray 1.70 X 1-159 [» ]
    3SRS X-ray 1.70 X 1-159 [» ]
    3SRU X-ray 1.70 X 1-159 [» ]
    3SRW X-ray 1.70 X 1-159 [» ]
    4FGG X-ray 2.30 A 1-159 [» ]
    4FGH X-ray 2.50 A 1-159 [» ]
    4LAE X-ray 1.69 X 1-159 [» ]
    4LAG X-ray 1.70 X 1-159 [» ]
    4LAH X-ray 1.88 X 1-159 [» ]
    4LEK X-ray 1.70 X 1-159 [» ]
    ProteinModelPortali P0A017.
    SMRi P0A017. Positions 2-158.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P0A017.
    ChEMBLi CHEMBL1681620.

    Proteomic databases

    PRIDEi P0A017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0262.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    Miscellaneous databases

    EvolutionaryTracei P0A017.

    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. "Characterization of the gene for chromosomal trimethoprim-sensitive dihydrofolate reductase of Staphylococcus aureus ATCC 25923."
      Dale G.E., Then R.L., Stueber D.
      Antimicrob. Agents Chemother. 37:1400-1405(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.
    2. "N-terminal amino acid sequence of the chromosomal dihydrofolate reductase purified from trimethoprim-resistant Staphylococcus aureus."
      Hartman P.G., Stahli M., Kocher H.P., Then R.L.
      FEBS Lett. 242:157-160(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-36.
      Strain: 157/4696.
    3. "Inhibitory properties and X-ray crystallographic study of the binding of AR-101, AR-102 and iclaprim in ternary complexes with NADPH and dihydrofolate reductase from Staphylococcus aureus."
      Oefner C., Parisi S., Schulz H., Lociuro S., Dale G.E.
      Acta Crystallogr. D 65:751-757(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-159.
    4. "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 (1.48 ANGSTROMS) IN COMPLEX WITH NADPH AND TRIMETHOPRIM.

    Entry informationi

    Entry nameiDYR_STAAU
    AccessioniPrimary (citable) accession number: P0A017
    Secondary accession number(s): P10167
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 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 chromosomal and is sensitive to trimethoprim.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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