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

Gene ID: 947552, updated on 6-Jul-2026
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
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; 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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties. Caban CE, et al. Biochemistry, 1976 Apr 6. PMID 4094
  2. Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system. Anderson WB, et al. Arch Biochem Biophys, 1971 Apr. PMID 4934180
  3. 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
  4. Multiple molecular forms of glutamine synthetase produced by enzyme catalyzed adenylation and deadenylylation reactions. Stadtman ER, et al. Adv Enzyme Regul, 1970. PMID 4921405
  5. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. Ebner E, et al. Eur J Biochem, 1970 Jul. PMID 4920894

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.
Submit: New GeneRIF Correction

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 EXP
Inferred from Experiment
more info
 PubMed 
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 L-glutamine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in regulation of L-glutamine biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in regulation of L-glutamine biosynthetic 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 
Preferred Names
fused glutamine synthetase deadenylase/glutamine synthetase adenylyltransferase
NP_417525.1

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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

    See identical proteins and their annotated locations for NP_417525.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A0H2Z3A4
    Conserved Domains (1) summary
    PRK11072
    Location:1 → 944
    PRK11072; bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase
Nucleotide Protein
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