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

    Gene ID: 946544, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hisH
    Official Full Name
    imidazole glycerol phosphate synthase subunit HisH
    Primary source
    ECOCYC:EG10450
    Locus tag
    b2023
    See related
    ASAP:ABE-0006722
    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
    ECK2018
    Summary
    N-terminus of purified HisH was sequenced by Klem and Davisson (1993), and the fMet is not clipped. [More information is available at EcoGene: EG10450]. 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: EG10450].
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    Genomic context

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    Sequence:
    NC_000913.3 (2094535..2095125)

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

    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. 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
    2. Histidine-requiring mutants of Escherichia coli K12. Garrick-Silversmith L, et al. Genetics, 1970 Oct. PMID 4934198, Free PMC Article
    3. Kinetic model of imidazologlycerol-phosphate synthetase from Escherichia coli. Demin OV, et al. Biochemistry (Mosc), 2004 Dec. PMID 15627387
    4. On the structure of hisH: protein structure prediction in the context of structural and functional genomics. O'Donoghue P, et al. J Struct Biol, 2001 May-Jun. PMID 11551184
    5. 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

    See all (22) 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.
    Submit: New GeneRIF Correction

    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 glutaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 pentosyltransferase 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
    		  
    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 HisH
    NP_416527.1

    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
      2094535..2095125
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416527.1 imidazole glycerol phosphate synthase subunit HisH [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416527.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6N8NJJ9, B1B4V3
      Conserved Domains (1) summary
      PRK13170
      Location:1 → 196
      hisH; imidazole glycerol phosphate synthase subunit HisH; Provisional
    Nucleotide Protein
    Heading Accession and Version

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