A0A162CU24 · A0A162CU24_9ENTR
- 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) | ||||
Sequence: K | ||||||
Binding site | 40 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 46 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 52 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 74 | Could play a key role in the communication between the regulatory and the substrate sites | ||||
Sequence: Q | ||||||
Site | 113 | Could play a key role in the communication between the regulatory and the substrate sites | ||||
Sequence: W | ||||||
Binding site | 114 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 130 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 179 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 194-195 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EK | ||||||
Binding site | 212 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 370 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 386 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 419-423 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: REMLR |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Enterobacter > Enterobacter cloacae complex
Accessions
- Primary accessionA0A162CU24
- Secondary accessions
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-291 | Nucleotidyl transferase | ||||
Sequence: ALILAGGRGTRLKDLTIKRAKPAVHFGGKFRIIDFALSNCLNSGIRRIGVITQYQSHTLVQHIQRGWSFFSEEMNEFVDLLPAQQRVHGENWYRGTADAVTQNLDIIRRYNAEYIVILAGDHIYKQDYSHMLIDHVEKGARCTVACLPVPVAEATAFGVMHVDADDKIIDFVEKPANPPTMPGDDTKSLASMGIYVFDADYLYELLEEDDKDENSSHDFGKDIIPKITKAGMAYAHPFPLSCVQSDPNAEPYWRDVGTLEAYWKANLDLA |
Sequence similarities
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)48,585
- Last updated2016-07-06 v1
- Checksum56A6F45EC367C4B3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LEES01000009 EMBL· GenBank· DDBJ | KLP60098.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LEDI01000024 EMBL· GenBank· DDBJ | KLQ03412.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAFKCP010000011 EMBL· GenBank· DDBJ | MBU3768223.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP056737 EMBL· GenBank· DDBJ | QLV17362.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FKDK01000016 EMBL· GenBank· DDBJ | SAB00231.1 EMBL· GenBank· DDBJ | Genomic DNA |