A0A6B3Q6J7 · A0A6B3Q6J7_ENTFC
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids339 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.
Catalytic activity
- sn-glycerol 3-phosphate + NAD+ = dihydroxyacetone phosphate + NADH + H+
Pathway
Membrane lipid metabolism; glycerophospholipid metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 9-14 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 12 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 13 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 107 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 107 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 107 | substrate | |||
Binding site | 138 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 140 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 142 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 142 | NADPH (UniProtKB | ChEBI) | |||
Active site | 193 | Proton acceptor | |||
Binding site | 193 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 246 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 256 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 257 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 257 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 257 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 257-258 | substrate | |||
Binding site | 258 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 281 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 283 | NADPH (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | glycerol-3-phosphate dehydrogenase (NADP+) activity | |
Molecular Function | glycerol-3-phosphate dehydrogenase [NAD(P)+] activity | |
Molecular Function | NAD binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | glycerol-3-phosphate biosynthetic process | |
Biological Process | glycerol-3-phosphate catabolic process | |
Biological Process | glycerophospholipid metabolic process | |
Biological Process | phospholipid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus
Accessions
- Primary accessionA0A6B3Q6J7
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-162 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 182-322 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | |||
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)36,640
- Last updated2020-06-17 v1
- MD5 ChecksumD724E1C8C2CFA756193E35E3A2F2C9F8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAAHCB010000081 EMBL· GenBank· DDBJ | NEU45874.1 EMBL· GenBank· DDBJ | Genomic DNA |