A0A2D7NNV9 · A0A2D7NNV9_UNCDE
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- Genegap
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids336 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
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 | 34 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 78 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 120 | 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 | 212-213 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 235 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 317 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | |
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Biological Process | glucose metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Myxococcota > Myxococcia
Accessions
- Primary accessionA0A2D7NNV9
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-153 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: INIGINGFGRIGRMVLRAGINNPNIRFVAINDLVPAENLAYLMKYDSTHGRFPGNVETDGNNILIDGKSIECVSERDPEQXGWGDKGVDYVIESTGLFTTLEKAELHLKAGAKKVVISAPAKSKEISTFVMGVNHETYQPSSDQVVSNASC |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)35,912
- Last updated2018-04-25 v1
- Checksum2158C9AF16AEF000