W0Z8A4 · W0Z8A4_9MICO
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids375 (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 | 15-20 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGSWG | ||||||
Binding site | 18 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 19 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 39 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 40 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 56 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 114 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | substrate | ||||
Sequence: K | ||||||
Binding site | 144 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 148 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 148 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 199 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 199 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 252 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 262 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 263 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 263 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 263 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 263-264 | substrate | ||||
Sequence: RN | ||||||
Binding site | 264 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 289 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Microbacterium
Accessions
- Primary accessionW0Z8A4
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-168 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: KVAVIGAGSWGTTFGKILADGGAAVTMWARRPELAHEIAEGKRNSEYLPGVNLPRSMTATAHLSEALDGATQIYLSVPSQALRESLKAVRPLVADNDALLISLMKGVERRSGMRMSQVIEQELACDPARIAVASGPNLALEIAREQPTAAVISSTSQET | ||||||
Domain | 188-327 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DVIGTEFGGVLKNLIAVAIGIVDGVGYGENTKASIITRGLVEMTDFAVAYGAQPETLQGLAGLGDLIATCQSPLSRNNTAGRLLGQGYSFQDVVKQMQQTAEGLASVAPVLQLAKEVGVEMPIVEQVKRVLDGTMKPQQI | ||||||
Region | 321-353 | Disordered | ||||
Sequence: TMKPQQIAPHLTTDDDTPRGERTQNAQTGGGGA |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)39,569
- Last updated2014-03-19 v1
- Checksum4462B72E4423132D
Keywords
- Technical term