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    glnE fused glutamine synthetase deadenylase/glutamine synthetase adenylyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947552, updated on 3-Dec-2024

    Summary

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    Official Symbol
    glnE
    Official Full Name
    fused glutamine synthetase deadenylase/glutamine synthetase adenylyltransferase
    Primary source
    ECOCYC:EG11602
    Locus tag
    b3053
    See related
    ASAP:ABE-0010018
    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
    ECK3043
    Summary
    GlnE has two homologous domains: the N-terminal domain is the deadenylase, and the C-terminal domain is the adenylase (Jaggi, 1997). [More information is available at EcoGene: EG11602].
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    Genomic context

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    Sequence:
    NC_000913.3 (3196801..3199641, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene toxic peptide IbsE Neighboring gene fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase Neighboring gene inorganic triphosphatase Neighboring gene putative signal transduction protein (SH3 domain)

    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. Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli. Jiang P, et al. Biochemistry, 2007 Apr 3. PMID 17355124
    2. Adenosine triphosphate: glutamine synthetase adenylyltransferase of Escherichia coli: two active molecular forms. Hennig SB, et al. Proc Natl Acad Sci U S A, 1970 Dec. PMID 4923119, Free PMC Article
    3. Multiple molecular forms of glutamine synthetase produced by enzyme catalyzed adenylation and deadenylylation reactions. Stadtman ER, et al. Adv Enzyme Regul, 1970. PMID 4921405
    4. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. Ebner E, et al. Eur J Biochem, 1970 Jul. PMID 4920894
    5. Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase. Xu Y, et al. Protein Expr Purif, 2004 Mar. PMID 14766310

    See all (47) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. investigation of regulation of UR-PII-ATase-GS bicyclic system: Data suggest that AT activity is only bound/activated by completely unmodified PII and that this design is largely responsible for ultrasensitivity of bicyclic system.
      Title: A source of ultrasensitivity in the glutamine response of the bicyclic cascade system controlling glutamine synthetase adenylylation state and activity in Escherichia coli.
    2. the adenylyl-removing (AR) activity of bifunctional GS adenylyltransferase/adenylyl-removing enzyme (ATase) is required to counterbalance its AT activity during steady-state growth under both nitrogen-excess and nitrogen-limiting conditions
      Title: Reversible adenylylation of glutamine synthetase is dynamically counterbalanced during steady-state growth of Escherichia coli.
    3. The structures of the adenylyl transferase and adenylyl removase domains overlap with an rmsd of 2.4 A when the superhelical R domain is omitted.
      Title: Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: evidence for gene duplication and evolution of a new active site.
    4. A panel of mAbs to adenylyltransferase was used to demonstrate that the cellular nitrogen status indicators, PII and PII-UMP, probably bind in the central regulatory domain to stimulate the adenylylation and deadenylylation reactions, respectively.
      Title: The domains carrying the opposing activities in adenylyltransferase are separated by a central regulatory domain.
    5. X-ray crystallographic analysis of the C-terminal domain of adenylyltransferase (ATase) from Escherichia coli
      Title: Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase.
    6. Subtle alterations in the environment of glutamine synthetase side chain residue Tyr-397 are sufficient to induce changes previously thought to require adenylylation.
      Title: Mutation of the adenylylated tyrosine of glutamine synthetase alters its catalytic properties.
    7. adenylyltransferase (AT) reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP.
      Title: Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate.
    8. N-terminal NT domain contains adenylyl-removing active site, & C-terminal NT domain has adenylyltransferase active site; enzyme has glutamine binding site, & glutamine increases affinity for PII; it contains multiple sites for binding of PII & PII-UMP
      Title: Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli.
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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables [glutamate-ammonia-ligase] adenylyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables [glutamate-ammonia-ligase] adenylyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables [glutamate-ammonia-ligase] adenylyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotidyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in regulation of glutamine family amino acid metabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in regulation of glutamine family amino acid metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of glutamine family amino acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    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

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    Preferred Names
    fused glutamine synthetase deadenylase/glutamine synthetase adenylyltransferase
    NP_417525.1

    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
      3196801..3199641 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417525.1 fused glutamine synthetase deadenylase/glutamine synthetase adenylyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417525.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8T5YAS0
      Conserved Domains (1) summary
      PRK11072
      Location:1 → 944
      PRK11072; bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase
    Nucleotide Protein
    Heading Accession and Version

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