A0A4R1AL85 · A0A4R1AL85_9ACTN
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids333 (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 | 11 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 12 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 32 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 33 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 49 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 106 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 106 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 106 | substrate | |||
Binding site | 136 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 140 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 140 | NADPH (UniProtKB | ChEBI) | |||
Active site | 191 | Proton acceptor | |||
Binding site | 191 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 244 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 254 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 255 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 255 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 255 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 255-256 | substrate | |||
Binding site | 256 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 279 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 281 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Aeromicrobium
Accessions
- Primary accessionA0A4R1AL85
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-17 | ||||
Chain | PRO_5038591444 | 18-333 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | ||
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 4-158 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 180-320 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | |||
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length333
- Mass (Da)35,046
- Last updated2019-07-31 v1
- MD5 ChecksumE2F2DA18523AD3B7FDE817BAFD84858A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SJXM01000014 EMBL· GenBank· DDBJ | TCI96760.1 EMBL· GenBank· DDBJ | Genomic DNA |