A0A1F0UCR0 · A0A1F0UCR0_9PAST
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids339 (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 + phosphate + NAD+ = (2R)-3-phospho-glyceroyl phosphate + NADH + H+
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: T | ||||||
Binding site | 149-151 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 150 | Nucleophile | ||||
Sequence: C | ||||||
Site | 177 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 180 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 209-210 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 232 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 319 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Haemophilus
Accessions
- Primary accessionA0A1F0UCR0
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-150 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: IKIGINGFGRIGRIVFRAAQHRDDIEVVGINDLIDVEYMAYMLKYDSTHGRFDGTVEVKDGNLVVNGKTIRVTSERDPANLNWGAIGVDVAVEATGLFLTDETARKHITAGAKKVVLTGPSKDSTPMFVRGVNFGAYAGQDIVSNASC | ||||||
Region | 186-205 | Disordered | ||||
Sequence: VDGPSAKDWRGGRGASQNII |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)36,114
- Last updated2017-02-15 v1
- ChecksumCC8060C63874F908