D5MLA3 · D5MLA3_METO1
- ProteinGlucose-1-phosphate adenylyltransferase
- GeneglgC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids417 (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
Pathway
Glycan biosynthesis; glycogen biosynthesis.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 57 | Could play a key role in the communication between the regulatory and the substrate sites | ||||
Sequence: Q | ||||||
Site | 95 | Could play a key role in the communication between the regulatory and the substrate sites | ||||
Sequence: W | ||||||
Binding site | 96 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 161 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 176-177 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: EK | ||||||
Binding site | 194 | alpha-D-glucose 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S |
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
- Taxonomic lineageBacteria > Candidatus Methylomirabilota > Candidatus Methylomirabilia > Candidatus Methylomirabilales > Candidatus Methylomirabilaceae > Candidatus Methylomirabilis
Accessions
- Primary accessionD5MLA3
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-276 | Nucleotidyl transferase | ||||
Sequence: GIIMAGGRGERLHPLTKDRAKPAVPFGGKYRIIDVVLSNFVNSGIYSIYVLTQFKAQSLVEHLQEGWQVTSVSRNHFVVPVPAQMRTGEDWYRGTADAVFQNVHLIKRVHPRVVAVFGADHIYKMNIRQMMEYHLRREAEVTVAALPVGIEEASHYGVMEADHTWRLLGFEEKPAQPKPIPGESEHALVSMGNYLFETDLLLRAVEEDAHDPHSTHDFGRDVLPRLVAEGRKVYAYDFRRNRIPTLLRGEEPSYWRDVGTIEAYYEANMDLR |
Sequence similarities
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length417
- Mass (Da)47,510
- Last updated2010-06-15 v1
- Checksum5288E63924CA58A3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FP565575 EMBL· GenBank· DDBJ | CBE67769.1 EMBL· GenBank· DDBJ | Genomic DNA |