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    folE GTP cyclohydrolase 1 [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 949040, updated on 2-May-2024

    Summary

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    Gene symbol
    folE
    Gene description
    GTP cyclohydrolase 1
    Primary source
    ASAP:ABE-0007117
    Locus tag
    b2153
    See related
    ECOCYC:EG11375
    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
    ECK2146
    Summary
    Although a folE null mutant could not be made by Baba (2006), leading to its inclusion in the set of 303 essential genes, Klaus (2005) were able to construct a deletion mutation in folE. [More information is available at EcoGene: EG11375]. GTP cyclohydrolase I is an allosteric enzyme that catalyzes the first step in the biosynthesis of tetrahydrofolate . [More information is available at EcoCyc: EG11375].
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    Genomic context

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    Sequence:
    NC_000913.3 (2242984..2243652, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional dual regulator GalS Neighboring gene DUF418 domain-containing protein YeiB Neighboring gene S-formylglutathione hydrolase/S-lactoylglutathione hydrolase Neighboring gene iron-catecholate outer membrane transporter CirA

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Biosynthesis of 7-deazaguanosine-modified tRNA nucleosides: a new role for GTP cyclohydrolase I. Phillips G, et al. J Bacteriol, 2008 Dec. PMID 18931107, Free PMC Article
    2. Biochemical characterization of oligomerization of Escherichia coli GTP cyclohydrolase I. Lee S, et al. J Biochem Mol Biol, 2002 May 31. PMID 12297008
    3. Reaction mechanism of GTP cyclohydrolase I: single turnover experiments using a kinetically competent reaction intermediate. Schramek N, et al. J Mol Biol, 2002 Feb 22. PMID 11866535
    4. Ring opening is not rate-limiting in the GTP cyclohydrolase I reaction. Schramek N, et al. J Biol Chem, 2001 Jan 26. PMID 11056154
    5. Structure and mechanism of GTP cyclohydrolase I of Escherichia coli. Nar H, et al. Biochem Soc Trans, 1996 Feb. PMID 8674705

    See all (33) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables GTP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables GTP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables GTP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables GTP cyclohydrolase I activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables GTP cyclohydrolase I activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables GTP cyclohydrolase I activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in one-carbon metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in organic cyclic compound biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within queuosine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tetrahydrobiopterin 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
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    GTP cyclohydrolase 1
    NP_416658.1

    NCBI Reference Sequences (RefSeq)

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    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
      2242984..2243652 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416658.1 GTP cyclohydrolase 1 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416658.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7QBC5
      Conserved Domains (1) summary
      cl00263
      Location:40 → 220
      TFold; Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl ...
    Nucleotide Protein
    Heading Accession and Version

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