A0A1R2AQ69 · A0A1R2AQ69_9CILI
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids343 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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 | 15-16 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 37 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 124 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 154-156 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 155 | Nucleophile | ||||
Sequence: C | ||||||
Site | 182 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 185 | 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
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Ciliophora > Postciliodesmatophora > Heterotrichea > Heterotrichida > Stentoridae > Stentor
Accessions
- Primary accessionA0A1R2AQ69
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-155 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: VKLGINGFGRIGRLVCRAAIENPYVEVVAINDPFMDVEYMAYQFKYDSVHGKYPQTVGTHEGKLIIGNKAIIVVCEKDPTNLPWDFLCIDYILECTGVFIDRKKCELHINAGARKVLLSSPSREDIPMFVMGVNQEKYTSDINIVSNASC |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length343
- Mass (Da)37,677
- Last updated2017-04-12 v1
- ChecksumD7015E5041040415
Keywords
- Technical term