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Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate, the immediate precursor of folate derivatives.1 Publication

Catalytic activityi

6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

Cofactori

Mg2+By similarity1 PublicationNote: Magnesium is required for activity, even if it seems to interact primarily with the substrate.Curated

Kineticsi

  1. KM=5.4 µM for 4-aminobenzoate1 Publication
  2. KM=9.3 µM for 6-hydroxymethyl-7,8-dihydropterin diphosphate1 Publication

    Pathwayi: tetrahydrofolate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Dihydropteroate synthase (folP), Dihydropteroate synthase (folP), Dihydropteroate synthase (CH51_02615), Dihydropteroate synthase (folP), Dihydropteroate synthase (folP), Dihydropteroate synthase (folP), Dihydropteroate synthase (AL077_11030), Dihydropteroate synthase (AL078_09425), Dihydropteroate synthase (RK97_01900)
    2. no protein annotated in this organism
    This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi11 – 111Magnesium1 Publication
    Binding sitei52 – 5216-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication
    Binding sitei84 – 8416-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication
    Binding sitei103 – 10316-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication
    Binding sitei167 – 16716-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication
    Binding sitei203 – 20316-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Antibiotic resistance, Folate biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.5.1.15. 3352.
    UniPathwayiUPA00077; UER00156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropteroate synthase1 Publication (EC:2.5.1.151 Publication)
    Short name:
    DHPS1 Publication
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    Gene namesi
    Name:folP
    Synonyms:dpsA1 Publication
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 267267Dihydropteroate synthasePRO_0000168225Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi93062.SACOL0558.

    Structurei

    Secondary structure

    1
    267
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117Combined sources
    Helixi14 – 163Combined sources
    Turni20 – 234Combined sources
    Helixi26 – 3813Combined sources
    Beta strandi42 – 487Combined sources
    Helixi60 – 7415Combined sources
    Beta strandi77 – 848Combined sources
    Helixi88 – 969Combined sources
    Beta strandi101 – 1044Combined sources
    Turni105 – 1084Combined sources
    Helixi114 – 1207Combined sources
    Beta strandi124 – 1285Combined sources
    Helixi139 – 15618Combined sources
    Helixi161 – 1633Combined sources
    Beta strandi164 – 1674Combined sources
    Helixi176 – 1849Combined sources
    Helixi186 – 1905Combined sources
    Beta strandi196 – 1983Combined sources
    Helixi204 – 2074Combined sources
    Beta strandi210 – 2123Combined sources
    Helixi216 – 2194Combined sources
    Helixi220 – 23314Combined sources
    Beta strandi237 – 2415Combined sources
    Helixi243 – 26220Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AD1X-ray2.20A/B2-267[»]
    1AD4X-ray2.40A/B2-267[»]
    ProteinModelPortaliO05701.
    SMRiO05701. Positions 2-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO05701.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 251251Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni239 – 24136-hydroxymethyl-7,8-dihydropterin diphosphate bindingCombined sources1 Publication

    Sequence similaritiesi

    Belongs to the DHPS family.Curated
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4105EEI. Bacteria.
    COG0294. LUCA.

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    InterProiIPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding_dom.
    [Graphical view]
    PfamiPF00809. Pterin_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 1 hit.
    TIGRFAMsiTIGR01496. DHPS. 1 hit.
    PROSITEiPS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O05701-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTKTKIMGIL NVTPDSFSDG GKFNNVESAV TRVKAMMDEG ADIIDVGGVS
    60 70 80 90 100
    TRPGHEMITV EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD
    110 120 130 140 150
    IINDQWAGLY DHRMFQVVAK YDAEIVLMHN GNGNRDEPVV EEMLTSLLAQ
    160 170 180 190 200
    AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA EVMARLDELV ATEYPVLLAT
    210 220 230 240 250
    SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV HNVELNAKLA
    260
    KGIDFLKENE NARHNFS
    Length:267
    Mass (Da):29,498
    Last modified:July 1, 1997 - v1
    Checksum:iF9FB01B1EAFBC275
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z84573 Genomic DNA. Translation: CAB06539.1.
    RefSeqiWP_000167936.1. NZ_LN626917.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z84573 Genomic DNA. Translation: CAB06539.1.
    RefSeqiWP_000167936.1. NZ_LN626917.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AD1X-ray2.20A/B2-267[»]
    1AD4X-ray2.40A/B2-267[»]
    ProteinModelPortaliO05701.
    SMRiO05701. Positions 2-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi93062.SACOL0558.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4105EEI. Bacteria.
    COG0294. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00156.
    BRENDAi2.5.1.15. 3352.

    Miscellaneous databases

    EvolutionaryTraceiO05701.

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    InterProiIPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding_dom.
    [Graphical view]
    PfamiPF00809. Pterin_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 1 hit.
    TIGRFAMsiTIGR01496. DHPS. 1 hit.
    PROSITEiPS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Structure and function of the dihydropteroate synthase from Staphylococcus aureus."
      Hampele I.C., D'Arcy A., Dale G.E., Kostrewa D., Nielsen J., Oefner C., Page M.G.P., Schoenfeld H.-J., Stueber D., Then R.L.
      J. Mol. Biol. 268:21-30(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE IONS AND HYDROXYMETHYLPTERIN DIPHOSPHATE, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 25923 / DSM 1104 / Seattle 1945 / FO 14462 / JCM 2413.

    Entry informationi

    Entry nameiDHPS_STAAU
    AccessioniPrimary (citable) accession number: O05701
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: December 9, 2015
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Specific mutations in this gene are a major cause of sulfonamide resistance in MRSA clinical isolates.1 Publication

    Keywords - Technical termi

    3D-structure

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.