A0A0B5E823 · A0A0B5E823_9TRYP
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- GenegGAPDH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids339 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- D-glyceraldehyde 3-phosphate + NAD+ + phosphate = (2R)-3-phospho-glyceroyl phosphate + H+ + NADH
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 | 39 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 135 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 166-168 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 167 | Nucleophile | ||||
Sequence: C | ||||||
Site | 195 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 198 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 227-228 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 250 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 336 | 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
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Strigomonadinae > Kentomonas
Accessions
- Primary accessionA0A0B5E823
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-167 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: VKVGINGFGRIGRMVFQSICEENLLGTEIDVVAVVDMSTDAEYFAYQMKYDTVHGKPSYTVEVAKSSPSVKKPDVLVVNGHKILCVKAQRSPADLPWGKLGVDYVIESTGLFTNKAKAEGHLKGGAKKVVISAPASGGAKTIVMGVNQQEYNPSSHNVVSNASC |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)36,440
- Last updated2015-04-01 v1
- ChecksumF97A78B0760B9746