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O05701

- DHPS_STAAU

UniProt

O05701 - DHPS_STAAU

Protein

Dihydropteroate synthase

Gene

folP

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide.1 Publication

    Catalytic activityi

    (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

    Cofactori

    Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi11 – 111Magnesium
    Binding sitei19 – 191Substrate
    Binding sitei84 – 841Substrate
    Binding sitei103 – 1031Substrate
    Binding sitei167 – 1671Substrate
    Binding sitei203 – 2031Substrate
    Binding sitei239 – 2391Substrate
    Binding sitei241 – 2411Substrate

    GO - Molecular functioni

    1. dihydropteroate synthase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. folic acid biosynthetic process Source: UniProtKB-KW
    2. response to antibiotic Source: UniProtKB-KW
    3. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Antibiotic resistance, Folate biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropteroate synthase (EC:2.5.1.15)
    Short name:
    DHPS
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    Gene namesi
    Name:folP
    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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
    Regioni51 – 522Substrate binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0294.

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    InterProiIPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding.
    [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

    MTKTKIMGIL NVTPDSFSDG GKFNNVESAV TRVKAMMDEG ADIIDVGGVS    50
    TRPGHEMITV EEELNRVLPV VEAIVGFDVK ISVDTFRSEV AEACLKLGVD 100
    IINDQWAGLY DHRMFQVVAK YDAEIVLMHN GNGNRDEPVV EEMLTSLLAQ 150
    AHQAKIAGIP SNKIWLDPGI GFAKTRNEEA EVMARLDELV ATEYPVLLAT 200
    SRKRFTKEMM GYDTTPVERD EVTAATTAYG IMKGVRAVRV HNVELNAKLA 250
    KGIDFLKENE NARHNFS 267
    Length:267
    Mass (Da):29,498
    Last modified:July 1, 1997 - v1
    Checksum:iF9FB01B1EAFBC275
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z84573 Genomic DNA. Translation: CAB06539.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z84573 Genomic DNA. Translation: CAB06539.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AD1 X-ray 2.20 A/B 2-267 [» ]
    1AD4 X-ray 2.40 A/B 2-267 [» ]
    ProteinModelPortali O05701.
    SMRi O05701. Positions 2-265.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0294.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .

    Miscellaneous databases

    EvolutionaryTracei O05701.

    Family and domain databases

    Gene3Di 3.20.20.20. 1 hit.
    InterProi IPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR000489. Pterin-binding.
    [Graphical view ]
    Pfami PF00809. Pterin_bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51717. SSF51717. 1 hit.
    TIGRFAMsi TIGR01496. DHPS. 1 hit.
    PROSITEi PS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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) IN COMPLEX WITH MANGANESE IONS; HYDROXYMETHYLPTERIN PYROPHOSPHATE, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
      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: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3