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P57696

- DHPS_NEIMC

UniProt

P57696 - DHPS_NEIMC

Protein

Dihydropteroate synthase

Gene

folP

Organism
Neisseria meningitidis serogroup C
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      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 bindingi25 – 251MagnesiumBy similarity
    Binding sitei33 – 331SubstrateBy similarity
    Binding sitei99 – 991SubstrateBy similarity
    Binding sitei119 – 1191SubstrateBy similarity
    Binding sitei190 – 1901SubstrateBy similarity
    Binding sitei227 – 2271SubstrateBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Binding sitei264 – 2641SubstrateBy 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

    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
    Synonyms:dhpS
    OrganismiNeisseria meningitidis serogroup C
    Taxonomic identifieri135720 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283Dihydropteroate synthasePRO_0000168219Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP57696.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 274257Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 672Substrate 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.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P57696-1 [UniParc]FASTAAdd to Basket

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    MARHVWQAGR FEIGLDKPKI MGIVNLTPDS FSDGGVYSQN AQTALAHAEQ    50
    LLKEGADILD IGGESTRSGA DYVSPEEEWA RVEPVLAEVA GWGVPISLDT 100
    RRTVIMEKAL ALGGIDIIND VAALNDEGAV ELLARQADTG ICLMHMQGLP 150
    KNMQINPKYQ DVVGEVARYL KARAAECIAA GIAPQRITLD PGFCFGKTLQ 200
    HNITLMRHLP ELMAETGYPL LIGVSRKSMI GELTGETDAA ARGHGSVAAA 250
    LAAVARGAKI VRVHDVKATA DALKAWEALG INL 283
    Length:283
    Mass (Da):30,167
    Last modified:September 26, 2001 - v2
    Checksum:iFE8D19EFA15FA034
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361V → A in strain: BT054.
    Natural varianti42 – 432QT → RI in strain: BT054.
    Natural varianti50 – 501Q → R in strain: BT054.
    Natural varianti68 – 681S → P in strain: BT054.
    Natural varianti96 – 961I → V in strain: BT054.
    Natural varianti104 – 1052VI → AV in strain: BT054.
    Natural varianti107 – 1071E → G in strain: BT054.
    Natural varianti125 – 1251N → T in strain: BT054.
    Natural varianti137 – 1371A → T in strain: BT054.
    Natural varianti151 – 1511K → E in strain: BT054.
    Natural varianti152 – 1521N → T in strain: MO124.
    Natural varianti174 – 1741A → S in strain: MO124.
    Natural varianti178 – 1781I → V in strain: BT054.
    Natural varianti188 – 1881T → I in strain: MO124.
    Natural varianti194 – 1941C → G in strain: BT054.
    Natural varianti194 – 1941C → GSG in strain: MO124.
    Natural varianti198 – 1981T → P in strain: MO124.
    Natural varianti204 – 2041T → A in strain: BT054 and MO124.
    Natural varianti218 – 2181Y → F in strain: BT054 and MO124.
    Natural varianti228 – 2281S → R in strain: BT054.
    Natural varianti229 – 2291M → T in strain: MO124.
    Natural varianti230 – 2301I → V in strain: BT054.
    Natural varianti237 – 2382TD → AN in strain: MO124.
    Natural varianti241 – 2411A → E in strain: MO124.
    Natural varianti243 – 2431G → V in strain: BT054 and MO124.
    Natural varianti253 – 2531A → S in strain: BT054 and MO124.
    Natural varianti259 – 2591K → Q in strain: BT054 and MO124.
    Natural varianti275 – 2751A → V in strain: BT054 and MO124.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68063 Genomic DNA. Translation: CAA48200.1.
    X68067 Genomic DNA. Translation: CAA48204.1.
    X68064 Genomic DNA. Translation: CAA48201.1.
    PIRiA57423.
    S25612.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68063 Genomic DNA. Translation: CAA48200.1 .
    X68067 Genomic DNA. Translation: CAA48204.1 .
    X68064 Genomic DNA. Translation: CAA48201.1 .
    PIRi A57423.
    S25612.

    3D structure databases

    ProteinModelPortali P57696.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .

    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.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transformational exchanges in the dihydropteroate synthase gene of Neisseria meningitidis: a novel mechanism for acquisition of sulfonamide resistance."
      Raadstroem P., Fermer C., Kristiansen B.-E., Jenkins A., Skoeld O., Swedberg G.
      J. Bacteriol. 174:6386-6393(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BT054 / Serogroup C / Serotype 15, BT227 / Serogroup C / Serotype 2a and CCUG 23102 / MO124 / Serogroup C / Serotype 15.

    Entry informationi

    Entry nameiDHPS_NEIMC
    AccessioniPrimary (citable) accession number: P57696
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 74 of the entry and version 2 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