A0A7W3EFT9 · A0A7W3EFT9_ESCFE
- ProteinGlucose-1-phosphate adenylyltransferase
- GeneglgC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids431 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Catalytic activity
- alpha-D-glucose 1-phosphate + ATP + H+ = ADP-alpha-D-glucose + diphosphate
Activity regulation
Allosterically activated by fructose-1,6-bisphosphate (F16BP) and inhibited by AMP.
Pathway
Glycan biosynthesis; glycogen biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 39 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 40 | AMP (UniProtKB | ChEBI) | |||
Binding site | 46 | AMP (UniProtKB | ChEBI) | |||
Binding site | 52 | AMP (UniProtKB | ChEBI) | |||
Site | 74 | Could play a key role in the communication between the regulatory and the substrate sites | |||
Site | 113 | Could play a key role in the communication between the regulatory and the substrate sites | |||
Binding site | 114 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | |||
Binding site | 130 | AMP (UniProtKB | ChEBI) | |||
Binding site | 179 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | |||
Binding site | 194-195 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | |||
Binding site | 212 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | |||
Binding site | 370 | AMP (UniProtKB | ChEBI) | |||
Binding site | 386 | AMP (UniProtKB | ChEBI) | |||
Binding site | 419-423 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | glucose-1-phosphate adenylyltransferase activity | |
Biological Process | glycogen biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlucose-1-phosphate adenylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A7W3EFT9
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)48,667
- Last updated2021-06-02 v1
- Checksum80373E450666CD74
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP055675 EMBL· GenBank· DDBJ | QLN02132.1 EMBL· GenBank· DDBJ | Genomic DNA |