A0A1V5M8U1 · A0A1V5M8U1_UNCT6
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA_1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids327 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 8-13 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 12 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 32 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 104 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 104 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 104 | substrate | |||
Binding site | 132 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 134 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 136 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 136 | NADPH (UniProtKB | ChEBI) | |||
Active site | 187 | Proton acceptor | |||
Binding site | 187 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 240 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 250 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 251 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 251 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 251 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 251-252 | substrate | |||
Binding site | 252 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 275 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 277 | 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 > Bacteria division TA06
Accessions
- Primary accessionA0A1V5M8U1
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-155 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 176-316 | 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
- Length327
- Mass (Da)33,628
- Last updated2017-06-07 v1
- Checksum4C8BA85B363F307C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MWAK01000343 EMBL· GenBank· DDBJ | OPZ89654.1 EMBL· GenBank· DDBJ | Genomic DNA |