A0A927BM45 · A0A927BM45_STRGL
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids336 (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 | 11-16 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 14 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 15 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 35 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 36 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 52 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 109 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 109 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 109 | substrate | |||
Binding site | 139 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 143 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 143 | NADPH (UniProtKB | ChEBI) | |||
Active site | 194 | Proton acceptor | |||
Binding site | 194 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 247 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 257 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 258 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 258 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 258 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 258-259 | substrate | |||
Binding site | 259 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 284 | NADPH (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A927BM45
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 6-163 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 183-323 | 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
- Length336
- Mass (Da)35,024
- Last updated2023-02-22 v1
- Checksum74808DCFF0130FB2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACWUS010000004 EMBL· GenBank· DDBJ | MBD2829764.1 EMBL· GenBank· DDBJ | Genomic DNA |