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P0DB09

- DHPS_STRPQ

UniProt

P0DB09 - DHPS_STRPQ

Protein

Dihydropteroate synthase

Gene

folP

Organism
Streptococcus pyogenes serotype M3 (strain SSI-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 21 (01 Oct 2014)
      Sequence version 1 (27 Jul 2011)
      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

    BioCyciRETL1328306-WGS:GSTH-2346-MONOMER.
    SPYO193567:GHDO-1016-MONOMER.
    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
    Ordered Locus Names:SPs0960
    OrganismiStreptococcus pyogenes serotype M3 (strain SSI-1)
    Taxonomic identifieri193567 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000002699: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Dihydropteroate synthasePRO_0000411342Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer or homotrimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP0DB09.
    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

    Phylogenomic databases

    HOGENOMiHOG000217509.
    KOiK00796.
    OMAiDKGSPDK.
    OrthoDBiEOG67T5P5.

    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.

    P0DB09-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIGKFVIEG NAAIMGILNV TPDSFSDGGS YTTVQKALDH VEQMIADGAK    50
    IIDVGGESTR PGCQFVSATD EIDRVVPVIK AIKENYDILI SIDTYKTETA 100
    RAALEAGADI LNDVWAGLYD GQMFALAAEY DAPIILMHNQ DEEVYQEVTQ 150
    DVCDFLGNRA QAALDAGVPK NNIWIDPGFG FAKSVQQNTE LLKRLDRVCQ 200
    LGYPVLFGIS RKRVVDALLG GNTKAKERDG ATAALSAYAL GKGCQIVRVH 250
    DVKANQDIVA VLSQLM 266
    Length:266
    Mass (Da):28,755
    Last modified:July 27, 2011 - v1
    Checksum:iB3F79D5BC5445ACD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000034 Genomic DNA. Translation: BAC64055.1.
    RefSeqiNP_802222.1. NC_004606.1.

    Genome annotation databases

    EnsemblBacteriaiBAC64055; BAC64055; BAC64055.
    GeneIDi1066224.
    KEGGisps:SPs0960.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000034 Genomic DNA. Translation: BAC64055.1 .
    RefSeqi NP_802222.1. NC_004606.1.

    3D structure databases

    ProteinModelPortali P0DB09.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC64055 ; BAC64055 ; BAC64055 .
    GeneIDi 1066224.
    KEGGi sps:SPs0960.

    Phylogenomic databases

    HOGENOMi HOG000217509.
    KOi K00796.
    OMAi DKGSPDK.
    OrthoDBi EOG67T5P5.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .
    BioCyci RETL1328306-WGS:GSTH-2346-MONOMER.
    SPYO193567:GHDO-1016-MONOMER.

    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. "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution."
      Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y., Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H., Hattori M., Hamada S.
      Genome Res. 13:1042-1055(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SSI-1.

    Entry informationi

    Entry nameiDHPS_STRPQ
    AccessioniPrimary (citable) accession number: P0DB09
    Secondary accession number(s): Q8K7K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 21 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

    Complete proteome

    Documents

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

    External Data

    Dasty 3