A0A120I024 · A0A120I024_9MICO
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids384 (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 | 24-29 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 27 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 28 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 48 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 49 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 65 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 122 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 122 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 122 | substrate | |||
Binding site | 152 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 156 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 156 | NADPH (UniProtKB | ChEBI) | |||
Active site | 207 | Proton acceptor | |||
Binding site | 207 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 260 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 270 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 271 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 271 | NADPH (UniProtKB | ChEBI) | |||
Binding site | 271 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 271-272 | substrate | |||
Binding site | 272 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 297 | NADPH (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 > Bacillati > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Microterricola
Accessions
- Primary accessionA0A120I024
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 20-176 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | |||
Domain | 196-335 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | |||
Region | 333-359 | Disordered | |||
Compositional bias | 347-356 | Basic and acidic residues | |||
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)40,403
- Last updated2016-04-13 v1
- MD5 Checksum6CB2FAE01B70BB0FE49277992BE85375
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 347-356 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP014145 EMBL· GenBank· DDBJ | AMB58157.1 EMBL· GenBank· DDBJ | Genomic DNA |