A0A0R2P1V7 · A0A0R2P1V7_9ACTN
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids334 (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 | 7-12 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 11 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 31 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 105 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 105 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 105 | substrate | |||
Binding site | 135 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 139 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 139 | NADPH (UniProtKB | ChEBI) | |||
Active site | 190 | Proton acceptor | |||
Binding site | 190 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 243 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 253 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 254 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 254 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 254 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 254-255 | substrate | |||
Binding site | 255 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 280 | NADPH (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | acyltransferase activity | |
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 > Actinomycetota > Actinomycetes > Actinomycetes incertae sedis > ac1 cluster
Accessions
- Primary accessionA0A0R2P1V7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 2-159 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 179-319 | 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
- Length334
- Mass (Da)35,096
- Last updated2016-01-20 v1
- MD5 ChecksumE4B6A1F1094EB495AE184977BD191DA9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LIAS01000035 EMBL· GenBank· DDBJ | KRO30978.1 EMBL· GenBank· DDBJ | Genomic DNA |