Q41595 · G3PC_TAXBA
- ProteinGlyceraldehyde-3-phosphate dehydrogenase, cytosolic
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids340 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity).
Miscellaneous
Plants contain two types of GAPDH: cytosolic forms which participate in glycolysis and chloroplast forms which participate in photosynthesis. All the forms are encoded by distinct genes.
Catalytic activity
- D-glyceraldehyde 3-phosphate + NAD+ + phosphate = (2R)-3-phospho-glyceroyl phosphate + H+ + NADH
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16-17 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 38 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 85 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 156-158 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 157 | Nucleophile | ||||
Sequence: C | ||||||
Site | 184 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 187 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 216-217 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 239 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 321 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | |
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Biological Process | glucose metabolic process | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase, cytosolic
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Pinopsida > Pinidae > Conifers II > Cupressales > Taxaceae > Taxus
Accessions
- Primary accessionQ41595
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000145619 | 1-340 | Glyceraldehyde-3-phosphate dehydrogenase, cytosolic | |||
Sequence: MGSTGKIKIGINGFGRIGRLVARVALQRDDIELVAVNDPFISTESLTSLFKYDSVHGQWKKHEVKVKDEKTLLFGEKHVAVFGCRNPEEIPWGEVGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLTIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSNKDWRGGRAAGFNIIPSSTGAAKAVGKVLPVLNGKLTGMCFRVPTQDVSVVDLTVKLEKSATYGEIKAAIKEESEGKLKGILGYTEDDVVSTDFIGDSRSSIFDAKAGIALNDNFVKLVSWYDNEWGYSSRVIDLIVHMDSTA |
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length340
- Mass (Da)36,673
- Last updated1996-11-01 v1
- Checksum427E1BA0F65ABC15