A0A2P6MKI6 · A0A2P6MKI6_ALKUR
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids349 (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
- NAD+ + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H+ + NADH
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) | ||||
Sequence: GAGSWG | ||||||
Binding site | 11 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 12 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 32 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 49 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 106 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 106 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 106 | substrate | ||||
Sequence: K | ||||||
Binding site | 134 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 136 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 138 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 138 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 189 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 189 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 242 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 252 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 253 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 253 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 253 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 253-254 | substrate | ||||
Sequence: RN | ||||||
Binding site | 254 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 277 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 279 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
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 > Bacillales > Bacillaceae > Alkalicoccus
Accessions
- Primary accessionA0A2P6MKI6
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-158 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: AVIGAGSWGTALALVLADNGLEVDLWARSEKQAEAMHSSRRNMRYLPGVELPEQIKPTASLETAVKDKDMIVLVVPTKAVREVLPALRPLLKEGAVIAHASKGIEPETHLRVSEVIAEELPGHPVACLSGPSHAEEVCKRQPTTVTSSSLHMET | ||||||
Domain | 178-319 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DLTGVEIGGSLKNIIAIGSGMTSGLGFGDNARAALMTRGLAEISRLGVKLGADPLTFSGLSGLGDLIVTCTSYHSRNWRAGNMIGKGMTINQVETEMGMVVEGVRTTKAAQQLAEKLDVEMPITSELYAVLFENKDVEEAVE | ||||||
Region | 330-349 | Disordered | ||||
Sequence: MEAPAVSRNTNRDPLDHFEP |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)37,694
- Last updated2018-05-23 v1
- Checksum7C74BC320BE00565
Keywords
- Technical term