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P0C0G0

- DHPS_STRPY

UniProt

P0C0G0 - DHPS_STRPY

Protein

Dihydropteroate synthase

Gene

folP

Organism
Streptococcus pyogenes
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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.

    Catalytic activityi

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

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi19 – 191MagnesiumBy similarity
    Binding sitei27 – 271SubstrateBy similarity
    Binding sitei93 – 931SubstrateBy similarity
    Binding sitei112 – 1121SubstrateBy similarity
    Binding sitei176 – 1761SubstrateBy similarity
    Binding sitei212 – 2121SubstrateBy similarity
    Binding sitei248 – 2481SubstrateBy similarity
    Binding sitei250 – 2501SubstrateBy similarity

    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

    SABIO-RKP0C0G0.
    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
    OrganismiStreptococcus pyogenes
    Taxonomic identifieri1314 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Dihydropteroate synthasePRO_0000168232Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer or homotrimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C0G0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 260249Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 602Substrate bindingBy similarity

    Sequence similaritiesi

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

    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.

    P0C0G0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIGKFVIDG NAAIMGILNV TPDSFSDGGS YTTVQKVLQQ VDQLIAGGAK    50
    IIDVGGESTR PGYQFVSAAD EIERVVPMIK AIKAKYDVLI SIDTYKTETA 100
    RAALEAGADI LNDVRAGLYD GEMLALAAEY DVPIILMHNQ KEEVYQDVTQ 150
    DVCDFLSARA QAAIDAGVPK DNIWIDPGFG FPKSVQHNME LLKGLDHVCQ 200
    LGYPVLFGIS RKGVVDALLG GNTKAKERDG ATAALSAYAL GKGCQLVRVH 250
    DVKANQEIVA VLSQLM 266
    Length:266
    Mass (Da):28,515
    Last modified:September 13, 2005 - v1
    Checksum:iC6BC402F07CFDF36
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000685 Genomic DNA. Translation: CAA04238.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000685 Genomic DNA. Translation: CAA04238.1 .

    3D structure databases

    ProteinModelPortali P0C0G0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .
    SABIO-RK P0C0G0.

    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. "Sulfonamide resistance in Streptococcus pyogenes is associated with differences in the amino acid sequence of its chromosomal dihydropteroate synthase."
      Swedberg G., Ringertz S., Skoeld O.
      Antimicrob. Agents Chemother. 42:1062-1067(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: G56.
    2. "Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance."
      Swedberg G., Fermer C., Skoeld O.
      Adv. Exp. Med. Biol. 338:555-558(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: G56.

    Entry informationi

    Entry nameiDHPS_STRPY
    AccessioniPrimary (citable) accession number: P0C0G0
    Secondary accession number(s): O33724
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3