A0A2W5MVP0 · A0A2W5MVP0_9BACT
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids330 (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 | 49 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 82 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 105 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 105 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 105 | substrate | |||
Binding site | 133 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 135 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 137 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 137 | NADPH (UniProtKB | ChEBI) | |||
Active site | 188 | Proton acceptor | |||
Binding site | 188 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 241 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 251 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 252 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 252 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 252 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 252-253 | substrate | |||
Binding site | 253 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 276 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 278 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bdellovibrionota > Bdellovibrionia > Bdellovibrionales > Pseudobdellovibrionaceae > Micavibrio
Accessions
- Primary accessionA0A2W5MVP0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-156 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 177-317 | 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
- Length330
- Mass (Da)34,582
- Last updated2018-09-12 v1
- Checksum203261C6A8878698
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QFQB01000056 EMBL· GenBank· DDBJ | PZQ45256.1 EMBL· GenBank· DDBJ | Genomic DNA |