Q95YJ4 · Q95YJ4_ASCSU
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- GeneAsEP36
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids340 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 13-14 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 35 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 157-159 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 158 | Nucleophile | ||||
Sequence: C | ||||||
Site | 185 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 188 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 217-218 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 240 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 322 | 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
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Ascaridomorpha > Ascaridoidea > Ascarididae > Ascaris
Accessions
- Primary accessionQ95YJ4
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-158 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: PKVGINGFGRIGRLVLRAAVEKDTVEVVAVNDPFINIDYMVYMFKYDSTHGRFKGDVHAEGGKLVVSTPGKATHHITVHNSKDPSEIAWSADGAEYVVESTGVFTTVEKASAHLKGGAKKVIISAPSADAPMFVMGVNEDKYDGANNHVISNASC |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length340
- Mass (Da)36,144
- Last updated2001-12-01 v1
- Checksum46545B706EF70608
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB058666 EMBL· GenBank· DDBJ | BAB68543.1 EMBL· GenBank· DDBJ | mRNA |