Q2U0J7 · HEPG_ASPOR
- ProteinGlyceraldehyde-3-phosphate dehydrogenase B
- GenehepG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids334 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Glyceraldehyde-3-phosphate dehydrogenase; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing (PubMed:30466366).
The GAPDPH hepG/gdpB shows much higher resistance to HA than the GAPDH gpdA located outside of the cluster, but it does not seem to act in self-resistance (PubMed:30466366).
The GAPDPH hepG/gdpB shows much higher resistance to HA than the GAPDH gpdA located outside of the cluster, but it does not seem to act in self-resistance (PubMed:30466366).
Catalytic activity
- D-glyceraldehyde 3-phosphate + NAD+ + phosphate = (2R)-3-phospho-glyceroyl phosphate + H+ + NADHThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.28 mM | glyceraldehyde-3-phosphate (GAP) |
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) | ||||
Sequence: RI | ||||||
Binding site | 34 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 149-151 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 150 | Nucleophile | ||||
Sequence: C | ||||||
Site | 177 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 180 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 209-210 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 232 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 314 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
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 | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase B
- EC number
- Short namesGAPDH
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionQ2U0J7
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Does not affect the biosynthesis of heptelidic acid.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450834 | 1-334 | Glyceraldehyde-3-phosphate dehydrogenase B | |||
Sequence: MTAKVGINGFGRIGRIVFRNSFSHENTEVVMVNDPFIEVQYAAYMLKYDSTHGNFEYDVHIDGDSIVVNGKKVKFYAEKDPAKIPWKDAGAEYIIESTGVFTTVEKASAHLQGGAKKVIISAPSADAPMYVMGVNEKTYAGADVVSNASCTTNCLAPLTKVLHERFGVVEGLMTAVHAYTATQKLVDAPSKKDWRGGRAAAQNLIPSSTGAAKAVGKVIPELQGKVTGMSIRVPTSNVSVVDLTCRLEKGASYEEIITAIKEAAQGELKGILDYTEDDVVSSDMKGNPHSSIVDIKAGISLNPNFLKIVSWYDNEWGYSRRVLDLTAYIASVGK |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length334
- Mass (Da)36,080
- Last updated2006-01-24 v1
- ChecksumD0618E15F55AA6CF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000055 EMBL· GenBank· DDBJ | BAE64918.1 EMBL· GenBank· DDBJ | Genomic DNA |