A0A927P747 · A0A927P747_9FIRM
- ProteinMultifunctional fusion protein
- Genepgk
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids647 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic activity
- (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 23-25 | substrate | |||
Binding site | 39 | substrate | |||
Binding site | 62-65 | substrate | |||
Binding site | 121 | substrate | |||
Binding site | 154 | substrate | |||
Binding site | 204 | ATP (UniProtKB | ChEBI) | |||
Binding site | 295 | ATP (UniProtKB | ChEBI) | |||
Binding site | 326 | ATP (UniProtKB | ChEBI) | |||
Binding site | 352-355 | ATP (UniProtKB | ChEBI) | |||
Binding site | 408-410 | substrate | |||
Active site | 493 | Electrophile | |||
Active site | 565 | Proton acceptor | |||
Binding site | 571 | substrate | |||
Binding site | 611 | substrate | |||
Binding site | 632-633 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ADP binding | |
Molecular Function | ATP binding | |
Molecular Function | phosphoglycerate kinase activity | |
Molecular Function | triose-phosphate isomerase activity | |
Biological Process | gluconeogenesis | |
Biological Process | glycolytic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameTriosephosphate isomerase
- EC number
- Short namesTIM ; TPI
- Alternative names
- Recommended namePhosphoglycerate kinase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales
Accessions
- Primary accessionA0A927P747
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length647
- Mass (Da)69,238
- Last updated2023-02-22 v1
- Checksum1043B9E1F38EC5AF
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SVHE01000149 EMBL· GenBank· DDBJ | MBE5774478.1 EMBL· GenBank· DDBJ | Genomic DNA |