Q829W3 · G3P2_STRAW
- ProteinGlyceraldehyde-3-phosphate dehydrogenase 2
- Genegap2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids335 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic activity
- D-glyceraldehyde 3-phosphate + NAD+ + phosphate = (2R)-3-phospho-glyceroyl phosphate + H+ + NADH
Activity regulation
Inhibited by pentalenolactone.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.33 mM | D-glyceraldehyde 3-phosphate |
kcat is 165 sec-1 with D-glyceraldehyde 3-phosphate.
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 | 12-13 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 35 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 79 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 152-154 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 153 | Nucleophile | ||||
Sequence: C | ||||||
Site | 180 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 183 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 184 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 198 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 211-212 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 234 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 316 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 2
- EC number
- Short namesGAPDH 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionQ829W3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000422015 | 1-335 | Glyceraldehyde-3-phosphate dehydrogenase 2 | |||
Sequence: MTIRVGINGFGRIGRNYFRALLEQGADIEIVAVNDLGDTATTAHLLKYDTILGRLKAEVTHTADTITVDGKTIKVFSERNPADIPWGELNVDIVIESTGIFTKKADAEKHIAGGAKKVLISAPASDEDITIVLGVNEDKYDPAKHNVISNASCTTNCVAPMAKVLDENFGIVKGLMTTIHAYTNDQRILDFPHKDLRRARAAAENIIPTTTGAAKATALVLPQLKGKMDGISMRVPVPTGSATDLVVEVSREVTKDEVNAAFKKAAEGELQGYLSYTEDPIVSSDIVGDPSSCTFDSAMTMVMEGTSVKILGWYDNEWGYSNRLVDLTVFVGNQL |
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)36,162
- Last updated2003-06-01 v1
- Checksum8A006B5A173776B7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000030 EMBL· GenBank· DDBJ | BAC74007.1 EMBL· GenBank· DDBJ | Genomic DNA |