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glgC glucose-1-phosphate adenylyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947942, updated on 25-Jun-2025
Official Symbol
glgC
Official Full Name
glucose-1-phosphate adenylyltransferase
Primary source
ECOCYC:EG10379
Locus tag
b3430
See related
ASAP:ABE-0011204
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
ECK3416
Summary
Glucose-1-phosphate adenylyltransferase catalyzes the rate-limiting first step in the biosynthesis of glycogen. [More information is available at EcoCyc: EG10379].
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Sequence:
NC_000913.3 (3568033..3569328, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene glycogen phosphorylase Neighboring gene glycogen synthase Neighboring gene limit dextrin alpha-1,6-glucohydrolase Neighboring gene 1,4-alpha-glucan branching enzyme Neighboring gene protein YhgO Neighboring gene protein YhgP

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. Leung P, et al. J Bacteriol, 1986 Jul. PMID 3013841, Free PMC Article
  2. Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli. Frueauf JB, et al. J Biol Chem, 2001 Dec 7. PMID 11567027
  3. Truncated forms of the recombinant Escherichia coli ADP-glucose pyrophosphorylase: the importance of the N-terminal region for allosteric activation and inhibition. Wu MX, et al. Arch Biochem Biophys, 2001 May 15. PMID 11339804
  4. The N-terminal region is important for the allosteric activation and inhibition of the Escherichia coli ADP-glucose pyrophosphorylase. Wu MX, et al. Arch Biochem Biophys, 1998 Oct 1. PMID 9750179
  5. A kinetic study of site-directed mutants of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 295 in allosteric regulation. Meyer CR, et al. Arch Biochem Biophys, 1998 Apr 15. PMID 9587413

See all (43) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A model has been proposed in which the energy reporters regulate ADP-glucose pyrophosphorylase catalytic activity by intra-protomer interactions and inter-protomer crosstalk, with a sensory motif and two regulatory loops playing a prominent role.
    Title: Structural Basis of Glycogen Biosynthesis Regulation in Bacteria.
  2. Using computational studies, site-directed mutagenesis, and kinetic characterization, we found a critical region for transmitting the allosteric signal in the Escherichia coli ADP-glucose pyrophosphorylase
    Title: Conserved residues of the Pro103-Arg115 loop are involved in triggering the allosteric response of the Escherichia coli ADP-glucose pyrophosphorylase.
  3. ADP-glucose pyrophosphorylase with a pentapeptide insertion between Leu(102) and Pro(103) was catalytically competent but insensitive to activation.
    Title: Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis.
  4. N-terminus verified by Edman degradation on mature peptide
    Title: Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose-protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase.
  5. Structural role of N-terminus in allosteric regulation of ADPglucose pyrophosphorylase was studied.
    Title: ADPglucose pyrophosphorylase's N-terminus: structural role in allosteric regulation.
  6. First detailed characterization of the sugar phosphate site and the three-dimensional structure of ADP-glucose pyrophosphorylase.
    Title: Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables AMP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables glucose-1-phosphate adenylyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables glucose-1-phosphate adenylyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables magnesium ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables nucleotidyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in glucan biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within glycogen biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within protein homotetramerization IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
part_of glucose-1-phosphate adenylyltransferase complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of glucose-1-phosphate adenylyltransferase complex IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
glucose-1-phosphate adenylyltransferase
NP_417888.1

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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
    3568033..3569328 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417888.1 glucose-1-phosphate adenylyltransferase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417888.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B9ACJ3, A0A8S7CKX0, A0A8T3UDF9
    Conserved Domains (1) summary
    PRK00725
    Location:5 → 429
    glgC; glucose-1-phosphate adenylyltransferase; Provisional
Nucleotide Protein
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