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P0AC13

- DHPS_ECOLI

UniProt

P0AC13 - DHPS_ECOLI

Protein

Dihydropteroate synthase

Gene

folP

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (08 Nov 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.1 Publication

    Catalytic activityi

    (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

    Cofactori

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi22 – 221Magnesium
    Binding sitei30 – 301Substrate
    Binding sitei96 – 961Substrate
    Binding sitei115 – 1151Substrate
    Binding sitei185 – 1851Substrate
    Binding sitei221 – 2211Substrate
    Binding sitei255 – 2551Substrate
    Binding sitei257 – 2571Substrate

    GO - Molecular functioni

    1. dihydropteroate synthase activity Source: EcoCyc
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. folic acid biosynthetic process Source: EcoCyc
    2. response to antibiotic Source: UniProtKB-KW
    3. response to drug Source: EcoliWiki
    4. 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

    BioCyciEcoCyc:H2PTEROATESYNTH-MONOMER.
    ECOL316407:JW3144-MONOMER.
    MetaCyc:H2PTEROATESYNTH-MONOMER.
    SABIO-RKP0AC13.
    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
    Ordered Locus Names:b3177, JW3144
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG50011. folP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282Dihydropteroate synthasePRO_0000168207Add
    BLAST

    Proteomic databases

    PaxDbiP0AC13.
    PRIDEiP0AC13.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AC13.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-47922N.
    IntActiP0AC13. 1 interaction.
    MINTiMINT-1268009.
    STRINGi511145.b3177.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Beta strandi8 – 114
    Beta strandi16 – 227
    Turni25 – 273
    Helixi29 – 335
    Helixi36 – 5015
    Beta strandi53 – 608
    Helixi71 – 8818
    Beta strandi92 – 965
    Helixi100 – 1089
    Beta strandi113 – 1164
    Turni117 – 1204
    Helixi125 – 1328
    Beta strandi136 – 1394
    Helixi157 – 17418
    Helixi179 – 1813
    Beta strandi182 – 1854
    Helixi194 – 2029
    Helixi204 – 2107
    Beta strandi214 – 2163
    Helixi222 – 2287
    Helixi232 – 2343
    Helixi236 – 24813
    Beta strandi252 – 2576
    Helixi259 – 27517

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AJ0X-ray2.00A1-282[»]
    1AJ2X-ray2.00A1-282[»]
    1AJZX-ray2.00A1-282[»]
    ProteinModelPortaliP0AC13.
    SMRiP0AC13. Positions 1-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AC13.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 267253Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni62 – 632Substrate binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0294.
    HOGENOMiHOG000217510.
    KOiK00796.
    OMAiDCWISVD.
    OrthoDBiEOG67T5P5.
    PhylomeDBiP0AC13.

    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.

    P0AC13-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLFAQGTSL DLSHPHVMGI LNVTPDSFSD GGTHNSLIDA VKHANLMINA    50
    GATIIDVGGE STRPGAAEVS VEEELQRVIP VVEAIAQRFE VWISVDTSKP 100
    EVIRESAKVG AHIINDIRSL SEPGALEAAA ETGLPVCLMH MQGNPKTMQE 150
    APKYDDVFAE VNRYFIEQIA RCEQAGIAKE KLLLDPGFGF GKNLSHNYSL 200
    LARLAEFHHF NLPLLVGMSR KSMIGQLLNV GPSERLSGSL ACAVIAAMQG 250
    AHIIRVHDVK ETVEAMRVVE ATLSAKENKR YE 282
    Length:282
    Mass (Da):30,615
    Last modified:November 8, 2005 - v1
    Checksum:i6230C8883796F59E
    GO

    Sequence cautioni

    The sequence AAA57978.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61Q → E AA sequence (PubMed:1657875)Curated
    Sequence conflicti77 – 771R → A in AAA97509. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281F → I in TS20; resistant to sulfonamide and temperature-sensitive.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491362.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76209; AAC76209; b3177.
    BAE77221; BAE77221; BAE77221.
    GeneIDi12932492.
    947691.
    KEGGiecj:Y75_p3097.
    eco:b3177.
    PATRICi32121772. VBIEscCol129921_3270.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A43326.
    RefSeqi NP_417644.4. NC_000913.3.
    YP_491362.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AJ0 X-ray 2.00 A 1-282 [» ]
    1AJ2 X-ray 2.00 A 1-282 [» ]
    1AJZ X-ray 2.00 A 1-282 [» ]
    ProteinModelPortali P0AC13.
    SMRi P0AC13. Positions 1-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47922N.
    IntActi P0AC13. 1 interaction.
    MINTi MINT-1268009.
    STRINGi 511145.b3177.

    Chemistry

    ChEMBLi CHEMBL4032.
    DrugBanki DB01298. Sulfacytine.
    DB00576. Sulfamethizole.
    DB00263. Sulfisoxazole.

    Proteomic databases

    PaxDbi P0AC13.
    PRIDEi P0AC13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76209 ; AAC76209 ; b3177 .
    BAE77221 ; BAE77221 ; BAE77221 .
    GeneIDi 12932492.
    947691.
    KEGGi ecj:Y75_p3097.
    eco:b3177.
    PATRICi 32121772. VBIEscCol129921_3270.

    Organism-specific databases

    EchoBASEi EB4304.
    EcoGenei EG50011. folP.

    Phylogenomic databases

    eggNOGi COG0294.
    HOGENOMi HOG000217510.
    KOi K00796.
    OMAi DCWISVD.
    OrthoDBi EOG67T5P5.
    PhylomeDBi P0AC13.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00156 .
    BioCyci EcoCyc:H2PTEROATESYNTH-MONOMER.
    ECOL316407:JW3144-MONOMER.
    MetaCyc:H2PTEROATESYNTH-MONOMER.
    SABIO-RK P0AC13.

    Miscellaneous databases

    EvolutionaryTracei P0AC13.
    PROi P0AC13.

    Gene expression databases

    Genevestigatori P0AC13.

    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. "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: C-167.
    2. "Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100."
      Dallas W.S., Gowen J.E., Ray P.H., Cox M.J., Dev I.K.
      J. Bacteriol. 174:5961-5970(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Wang R., Kushner S.R.
      Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100."
      Talarico T.L., Dev I.K., Dallas W.S., Ferone R., Ray P.H.
      J. Bacteriol. 173:7029-7032(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-28.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    7. "Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog."
      Swedberg G., Castensson S., Skold O.
      J. Bacteriol. 137:129-136(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
      Strain: C-167.
    8. "Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase."
      Achari A., Somers D.O., Champness J.N., Bryant P.K., Rosemond J., Stammers D.K.
      Nat. Struct. Biol. 4:490-497(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH MANGANESE IONS; SULFANILAMIDE AND 7,8-DIHYDROPTERIN PYROPHOSPHATE ANALOGS, SUBUNIT.

    Entry informationi

    Entry nameiDHPS_ECOLI
    AccessioniPrimary (citable) accession number: P0AC13
    Secondary accession number(s): P26282, P78110, Q2M935
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 80 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, 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

    External Data

    Dasty 3