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    hisF imidazole glycerol phosphate synthase subunit HisF [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946516, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hisF
    Official Full Name
    imidazole glycerol phosphate synthase subunit HisF
    Primary source
    ECOCYC:EG10448
    Locus tag
    b2025
    See related
    ASAP:ABE-0006727
    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
    ECK2020
    Summary
    N-terminus of purified HisF was sequenced by Klem and Davisson (1993), and the fMet is not clipped. [More information is available at EcoGene: EG10448]. Imidazole glycerol phosphate synthase (HisFH) is a heterodimer that carries out the fifth step in histidine biosynthesis, as well as generating aminoimidazole carboxamide ribonucleotide, an intermediate in purine nucleotide biosynthesis. [More information is available at EcoCyc: EG10448].
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    Genomic context

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    Sequence:
    NC_000913.3 (2095844..2096620)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene histidinal/histidinol dehydrogenase Neighboring gene histidinol-phosphate aminotransferase Neighboring gene imidazoleglycerol-phosphate dehydratase/histidinol-phosphatase Neighboring gene imidazole glycerol phosphate synthase subunit HisH Neighboring gene 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase Neighboring gene putative bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase Neighboring gene O-antigen co-polymerase Neighboring gene UDP-glucose 6-dehydrogenase

    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. Nanometer propagation of millisecond motions in V-type allostery. Lipchock JM, et al. Structure, 2010 Dec 8. PMID 21134639, Free PMC Article
    2. In vivo evaluation of the interaction between the Escherichia coli IGP synthase subunits using the Bacterial Two-Hybrid system. Chioccioli S, et al. FEMS Microbiol Lett, 2020 Jul 1. PMID 32614412
    3. Suppression of the pleiotropic effects of HisH and HisF overproduction identifies four novel loci on the Salmonella typhimurium chromosome: osmH, sfiW, sfiX, and sfiY. Flores A, et al. J Bacteriol, 1995 Sep. PMID 7665459, Free PMC Article
    4. Excess histidine enzymes cause AICAR-independent filamentation in Escherichia coli. Frandsen N, et al. Mol Gen Genet, 1993 Sep. PMID 8413183
    5. Histidine-requiring mutants of Escherichia coli K12. Garrick-Silversmith L, et al. Genetics, 1970 Oct. PMID 4934198, Free PMC Article

    See all (25) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. In vivo evaluation of the interaction between the Escherichia coli IGP synthase subunits using the Bacterial Two-Hybrid system.
      Title: In vivo evaluation of the interaction between the Escherichia coli IGP synthase subunits using the Bacterial Two-Hybrid system.
    2. Enzyme activation in the ternary complex is primarily due to an enhancement of ms motions that allows formation of a population of enzymatically active conformers.
      Title: Nanometer propagation of millisecond motions in V-type allostery.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables imidazoleglycerol-phosphate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables imidazoleglycerol-phosphate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables imidazoleglycerol-phosphate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within L-histidine biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in L-histidine biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in L-histidine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of imidazoleglycerol-phosphate synthase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of imidazoleglycerol-phosphate synthase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    imidazole glycerol phosphate synthase subunit HisF
    NP_416529.1

    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
      2095844..2096620
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416529.1 imidazole glycerol phosphate synthase subunit HisF [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416529.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A828P6I4
      Conserved Domains (1) summary
      PRK02083
      Location:1 → 257
      PRK02083; imidazole glycerol phosphate synthase subunit HisF; Provisional
    Nucleotide Protein
    Heading Accession and Version

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