U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    folP dihydropteroate synthase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947691, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    folP
    Official Full Name
    dihydropteroate synthase
    Primary source
    ECOCYC:EG50011
    Locus tag
    b3177
    See related
    ASAP:ABE-0010441
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    dhpS; ECK3166
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (3324063..3324911, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene tRNA-Leu Neighboring gene Sec translocon subunit SecG Neighboring gene phosphoglucosamine mutase Neighboring gene ATP-dependent zinc metalloprotease FtsH Neighboring gene 23S rRNA 2'-O-ribose U2552 methyltransferase

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Adaptation to sulfonamide resistance in Neisseria meningitidis may have required compensatory changes to retain enzyme function: kinetic analysis of dihydropteroate synthases from N. meningitidis expressed in a knockout mutant of Escherichia coli. Fermér C, et al. J Bacteriol, 1997 Feb. PMID 9006040, Free PMC Article
    2. Point mutations in the dihydropteroate synthase gene causing sulfonamide resistance. Swedberg G, et al. Adv Exp Med Biol, 1993. PMID 8304179
    3. Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog. Swedberg G, et al. J Bacteriol, 1979 Jan. PMID 368012, Free PMC Article
    4. Characterization of mutations contributing to sulfathiazole resistance in Escherichia coli. Vedantam G, et al. Antimicrob Agents Chemother, 1998 Jan. PMID 9449266, Free PMC Article
    5. Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100. Dallas WS, et al. J Bacteriol, 1992 Sep. PMID 1522070, Free PMC Article

    See all (16) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on complete protein
      Title: Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100.
    Submit: New GeneRIF Correction

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables dihydropteroate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables dihydropteroate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dihydropteroate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in folic acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within folic acid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in folic acid-containing compound biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within response to xenobiotic stimulus EXP
    Inferred from Experiment
    more info
    		 PubMed 
    acts_upstream_of_or_within response to xenobiotic stimulus IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tetrahydrofolate biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tetrahydrofolate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    dihydropteroate synthase
    NP_417644.4

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      3324063..3324911 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417644.4 dihydropteroate synthase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417644.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7JTQ3
      Conserved Domains (1) summary
      PRK11613
      Location:1 → 282
      folP; dihydropteroate synthase; Provisional
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.