U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    folC bifunctional folylpolyglutamate synthetase/dihydrofolate synthetase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945451, updated on 17-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    folC
    Official Full Name
    bifunctional folylpolyglutamate synthetase/dihydrofolate synthetase
    Primary source
    ECOCYC:EG10327
    Locus tag
    b2315
    See related
    ASAP:ABE-0007645
    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
    dedC; ECK2309
    Summary
    folC codes for a bifunctional polypeptide. [More information is available at EcoCyc: EG10327].
    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 (2431674..2432942, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene amidophosphoribosyltransferase Neighboring gene colicin V production protein Neighboring gene cell division protein DedD Neighboring gene acetyl-CoA carboxyltransferase subunit beta Neighboring gene DedA family protein DedA

    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. Partial purification and properties of an enzyme from Escherichia coli that catalyzes the conversion of glutamic acid and 10-formyltetrahydropteroylglutamic acid to 10-formyltetrahydropterol-gamma-glutamyglutamic acid. Masurekar M, et al. Biochemistry, 1975 Jun 3. PMID 1095054
    2. Replacement of the folC gene, encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli, with genes mutagenized in vitro. Pyne C, et al. J Bacteriol, 1992 Mar. PMID 1548226, Free PMC Article
    3. A domino effect in antifolate drug action in Escherichia coli. Kwon YK, et al. Nat Chem Biol, 2008 Oct. PMID 18724364, Free PMC Article
    4. Mutagenesis of folylpolyglutamate synthetase indicates that dihydropteroate and tetrahydrofolate bind to the same site. Sheng Y, et al. Biochemistry, 2008 Feb 26. PMID 18232714
    5. Characterization of a mutation affecting the function of Escherichia coli folylpolyglutamate synthetase-dihydrofolate synthetase and further mutations produced in vitro at the same locus. Keshavjee K, et al. J Biol Chem, 1991 Oct 25. PMID 1939056

    See all (20) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The uridylyltransferase GlnD and tRNA modification GTPase MnmE allosterically control Escherichia coli folylpoly-gamma-glutamate synthase FolC.
      Title: The uridylyltransferase GlnD and tRNA modification GTPase MnmE allosterically control Escherichia coli folylpoly-γ-glutamate synthase FolC.
    2. mutagenesis study to identify structural elements of folylpolyglutamate synthetase that are directly responsible for the functional differences between the E. coli and the Lactobacillus casei enzymes
      Title: Mutagenesis of folylpolyglutamate synthetase indicates that dihydropteroate and tetrahydrofolate bind to the same site.
    3. N-terminus verified by Edman degradation on complete protein
      Title: Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene.
    4. analysis of an unexpected dihydrofolate binding site in Escherichia coli FolC
      Title: Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.
    Submit: New GeneRIF Correction

    Pathways from PubChem

    Go to the top of the page

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acid-amino acid ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydrofolate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables dihydrofolate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dihydrofolate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables guanosine tetraphosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tetrahydrofolylpolyglutamate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables tetrahydrofolylpolyglutamate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables tetrahydrofolylpolyglutamate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within 10-formyltetrahydrofolate biosynthetic process EXP
    Inferred from Experiment
    more info
    		 PubMed 
    acts_upstream_of_or_within dihydrofolate biosynthetic process EXP
    Inferred from Experiment
    more info
    		 PubMed 
    acts_upstream_of_or_within folic acid biosynthetic process EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in folic acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in folic acid-containing compound biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in folic acid-containing compound biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in one-carbon metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tetrahydrofolate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within tetrahydrofolylpolyglutamate biosynthetic process EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in tetrahydrofolylpolyglutamate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    bifunctional folylpolyglutamate synthetase/dihydrofolate synthetase
    NP_416818.1

    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
      2431674..2432942 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416818.1 bifunctional folylpolyglutamate synthetase/dihydrofolate synthetase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416818.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A7A6XMD7
      Conserved Domains (1) summary
      PRK10846
      Location:1 → 416
      PRK10846; bifunctional folylpolyglutamate synthase/ dihydrofolate 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.