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Protein

Dihydropteroate synthase

Gene

folP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.1 Publication

Catalytic activityi

6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.2 Publications

Cofactori

Mg2+1 PublicationNote: Magnesium is required for activity, even if it seems to interact primarily with the substrate.Curated1 Publication

Kineticsi

  1. KM=2.5 µM for 4-aminobenzoate1 Publication

    pH dependencei

    Optimum pH is 8.5.1 Publication

    Pathwayi: tetrahydrofolate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Dihydropteroate synthase (folP)
    2. Dihydrofolate synthase/folylpolyglutamate synthase (folC)
    This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi22MagnesiumBy similarity1
    Binding sitei626-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
    Binding sitei966-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
    Binding sitei1156-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
    Binding sitei1856-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
    Binding sitei2216-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1

    GO - Molecular functioni

    • dihydropteroate synthase activity Source: EcoliWiki
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • folic acid biosynthetic process Source: EcoCyc
    • response to drug Source: EcoliWiki
    • tetrahydrofolate biosynthetic process Source: GO_Central

    Keywordsi

    Molecular functionTransferase
    Biological processFolate biosynthesis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:H2PTEROATESYNTH-MONOMER
    MetaCyc:H2PTEROATESYNTH-MONOMER
    BRENDAi2.5.1.15 2167
    SABIO-RKiP0AC13
    UniPathwayiUPA00077; UER00156

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropteroate synthase1 Publication (EC:2.5.1.151 Publication)
    Short name:
    DHPS1 Publication
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    Gene namesi
    Name:folP
    Synonyms:dhpS
    Ordered Locus Names:b3177, JW3144
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG50011 folP

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL2364668
    DrugBankiDB00634 Sulfacetamide
    DB01298 Sulfacytine
    DB01581 Sulfamerazine
    DB01582 Sulfamethazine
    DB00576 Sulfamethizole
    DB01015 Sulfamethoxazole
    DB00259 Sulfanilamide
    DB06729 Sulfaphenazole
    DB00263 Sulfisoxazole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001682071 – 282Dihydropteroate synthaseAdd BLAST282

    Proteomic databases

    PaxDbiP0AC13
    PRIDEiP0AC13

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi4261486, 17 interactors
    DIPiDIP-47922N
    IntActiP0AC13, 1 interactor
    STRINGi316385.ECDH10B_3351

    Chemistry databases

    BindingDBiP0AC13

    Structurei

    Secondary structure

    1282
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 5Combined sources4
    Beta strandi8 – 11Combined sources4
    Beta strandi16 – 22Combined sources7
    Turni25 – 27Combined sources3
    Helixi29 – 33Combined sources5
    Helixi36 – 50Combined sources15
    Beta strandi53 – 60Combined sources8
    Helixi71 – 88Combined sources18
    Beta strandi92 – 96Combined sources5
    Helixi100 – 108Combined sources9
    Beta strandi113 – 116Combined sources4
    Turni117 – 120Combined sources4
    Helixi125 – 132Combined sources8
    Beta strandi136 – 139Combined sources4
    Helixi157 – 174Combined sources18
    Helixi179 – 181Combined sources3
    Beta strandi182 – 185Combined sources4
    Helixi194 – 202Combined sources9
    Helixi204 – 210Combined sources7
    Beta strandi214 – 216Combined sources3
    Helixi222 – 228Combined sources7
    Helixi232 – 234Combined sources3
    Helixi236 – 248Combined sources13
    Beta strandi252 – 257Combined sources6
    Helixi259 – 275Combined sources17

    3D structure databases

    ProteinModelPortaliP0AC13
    SMRiP0AC13
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AC13

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini15 – 267Pterin-bindingPROSITE-ProRule annotationAdd BLAST253

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni255 – 2576-hydroxymethyl-7,8-dihydropterin diphosphate bindingCombined sources1 Publication3

    Sequence similaritiesi

    Belongs to the DHPS family.Curated

    Phylogenomic databases

    eggNOGiENOG4105EEI Bacteria
    COG0294 LUCA
    HOGENOMiHOG000217510
    InParanoidiP0AC13
    KOiK00796
    OMAiWAVRVHD
    PhylomeDBiP0AC13

    Family and domain databases

    CDDicd00739 DHPS, 1 hit
    Gene3Di3.20.20.20, 1 hit
    InterProiView protein in InterPro
    IPR006390 DHP_synth
    IPR011005 Dihydropteroate_synth-like
    IPR000489 Pterin-binding_dom
    PfamiView protein in Pfam
    PF00809 Pterin_bind, 1 hit
    SUPFAMiSSF51717 SSF51717, 1 hit
    TIGRFAMsiTIGR01496 DHPS, 1 hit
    PROSITEiView protein in PROSITE
    PS00792 DHPS_1, 1 hit
    PS00793 DHPS_2, 1 hit
    PS50972 PTERIN_BINDING, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0AC13-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA
    60 70 80 90 100
    GATIIDVGGE STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP
    110 120 130 140 150
    EVIRESAKVG AHIINDIRSL SEPGALEAAA ETGLPVCLMH MQGNPKTMQE
    160 170 180 190 200
    APKYDDVFAE VNRYFIEQIA RCEQAGIAKE KLLLDPGFGF GKNLSHNYSL
    210 220 230 240 250
    LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL ACAVIAAMQG
    260 270 280
    AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE
    Length:282
    Mass (Da):30,615
    Last modified:November 8, 2005 - v1
    Checksum:i6230C8883796F59E
    GO

    Sequence cautioni

    The sequence AAA57978 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti6Q → E AA sequence (PubMed:1657875).Curated1
    Sequence conflicti77R → A in AAA97509 (Ref. 3) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti28F → I in TS20; resistant to sulfonamide and temperature-sensitive. 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X68776 Genomic DNA Translation: CAA48676.1
    X68777 Genomic DNA Translation: CAA48677.1
    L06494 Genomic DNA Translation: AAA23804.1
    L12968 Unassigned DNA Translation: AAA16123.1
    U01376 Genomic DNA Translation: AAA97509.1
    U18997 Genomic DNA Translation: AAA57978.1 Different initiation.
    U00096 Genomic DNA Translation: AAC76209.2
    AP009048 Genomic DNA Translation: BAE77221.1
    PIRiA43326
    RefSeqiNP_417644.4, NC_000913.3
    WP_000764731.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC76209; AAC76209; b3177
    BAE77221; BAE77221; BAE77221
    GeneIDi947691
    KEGGiecj:JW3144
    eco:b3177
    PATRICifig|1411691.4.peg.3555

    Similar proteinsi

    Entry informationi

    Entry nameiDHPS_ECOLI
    AccessioniPrimary (citable) accession number: P0AC13
    Secondary accession number(s): P26282, P78110, Q2M935
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: March 28, 2018
    This is version 108 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

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