A0A0W0CA22 · A0A0W0CA22_CANGB
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids332 (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 | 11-12 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 33 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 78 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 120 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 149-151 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Active site | 150 | Nucleophile | |||
Site | 177 | Activates thiol group during catalysis | |||
Binding site | 180 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 209-210 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 232 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 314 | NAD+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | external encapsulating structure | |
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Nakaseomyces
Accessions
- Primary accessionA0A0W0CA22
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 2-150 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | |||
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length332
- Mass (Da)35,879
- Last updated2016-03-16 v1
- Checksum43B6A0679A3F681C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LLZZ01000110 EMBL· GenBank· DDBJ | KTB06197.1 EMBL· GenBank· DDBJ | Genomic DNA |