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P59655

- DHPS_STRR6

UniProt

P59655 - DHPS_STRR6

Protein

Dihydropteroate synthase

Gene

sulA

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (30 Apr 2003)
      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.

    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 bindingi17 – 171MagnesiumBy similarity
    Binding sitei25 – 251Substrate
    Binding sitei91 – 911Substrate
    Binding sitei110 – 1101Substrate
    Binding sitei201 – 2011Substrate
    Binding sitei237 – 2371Substrate
    Binding sitei282 – 2821Substrate
    Binding sitei284 – 2841Substrate

    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

    BioCyciSPNE171101:GJC8-273-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:sulA
    Ordered Locus Names:spr0266
    OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
    Taxonomic identifieri171101 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000586: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Dihydropteroate synthasePRO_0000168231Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi171101.spr0266.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 177
    Helixi31 – 4414
    Beta strandi48 – 536
    Helixi63 – 8321
    Beta strandi87 – 915
    Helixi95 – 1039
    Beta strandi108 – 1114
    Turni112 – 1154
    Helixi121 – 1288
    Beta strandi131 – 1355
    Helixi138 – 1414
    Turni146 – 1505
    Helixi166 – 1705
    Helixi173 – 19119
    Helixi195 – 1973
    Beta strandi198 – 2014
    Helixi210 – 2189
    Helixi220 – 2245
    Turni225 – 2273
    Beta strandi230 – 2334
    Helixi238 – 2469
    Helixi256 – 27520
    Beta strandi279 – 2846
    Helixi286 – 30015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VEFX-ray1.80A/B1-314[»]
    2VEGX-ray2.40A/B1-314[»]
    ProteinModelPortaliP59655.
    SMRiP59655. Positions 7-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP59655.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 294285Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni57 – 582Substrate bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0294.
    HOGENOMiHOG000217509.
    KOiK00796.
    OMAiSALAGWH.
    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.

    P59655-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKANHAKT VICGIINVTP DSFSDGGQFF ALEQALQQAR KLIAEGASML    50
    DIGGESTRPG SSYVEIEEEI QRVVPVIKAI RKESDVLISI DTWKSQVAEA 100
    ALAAGADLVN DITGLMGDEK MPHVVAEARA QVVIMFNPVM ARPQHPSSLI 150
    FPHFGFGQAF TEEELADFET LPIEELMEAF FERALARAAE AGIAPENILL 200
    DPGIGFGLTK KENLLLLRDL DKLHQKGYPI FLGVSRKRFV INILEENGFE 250
    VNPETELGFR NRDTASAHVT SIAARQGVEV VRVHDVASHR MAVEIASAIR 300
    LADEAENLDL KQYK 314
    Length:314
    Mass (Da):34,418
    Last modified:April 30, 2003 - v1
    Checksum:iC7CEDD0C2EDAA061
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99070.1.
    RefSeqiNP_357860.1. NC_003098.1.

    Genome annotation databases

    EnsemblBacteriaiAAK99070; AAK99070; spr0266.
    GeneIDi934662.
    KEGGispr:spr0266.
    PATRICi19700365. VBIStrPne107296_0303.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99070.1 .
    RefSeqi NP_357860.1. NC_003098.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VEF X-ray 1.80 A/B 1-314 [» ]
    2VEG X-ray 2.40 A/B 1-314 [» ]
    ProteinModelPortali P59655.
    SMRi P59655. Positions 7-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 171101.spr0266.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK99070 ; AAK99070 ; spr0266 .
    GeneIDi 934662.
    KEGGi spr:spr0266.
    PATRICi 19700365. VBIStrPne107296_0303.

    Phylogenomic databases

    eggNOGi COG0294.
    HOGENOMi HOG000217509.
    KOi K00796.
    OMAi SALAGWH.
    OrthoDBi EOG67T5P5.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .
    BioCyci SPNE171101:GJC8-273-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P59655.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-255 / R6.
    2. "Dihydropteroate synthase from Streptococcus pneumoniae: structure, ligand recognition and mechanism of sulfonamide resistance."
      Levy C., Minnis D., Derrick J.P.
      Biochem. J. 412:379-388(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH PTERIN-6-YL-METHYL-MONOPHOSPHATE, SUBUNIT, FUNCTION.

    Entry informationi

    Entry nameiDHPS_STRR6
    AccessioniPrimary (citable) accession number: P59655
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 76 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, Complete proteome, Reference proteome

    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