A0A6I2F4E2 · A0A6I2F4E2_9MICO
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- Genegap
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids333 (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+
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) | |||
Binding site | 35 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 79 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 152-154 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Active site | 153 | Nucleophile | |||
Site | 180 | Activates thiol group during catalysis | |||
Binding site | 183 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 211-212 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 234 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 315 | NAD+ (UniProtKB | ChEBI) | |||
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
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Agromyces
Accessions
- Primary accessionA0A6I2F4E2
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-153 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | |||
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length333
- Mass (Da)35,088
- Last updated2020-08-12 v1
- Checksum5E307A2DC6C2BB92
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
WJIF01000002 EMBL· GenBank· DDBJ | MRG59459.1 EMBL· GenBank· DDBJ | Genomic DNA |