A0A4Y6UT54 · A0A4Y6UT54_SACBS
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids346 (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 | 12 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 13 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 33 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 107 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 107 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 107 | substrate | ||||
Sequence: K | ||||||
Binding site | 137 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 139 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 141 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 141 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 192 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 192 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 245 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 255 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 256 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 256 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 256 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 256-257 | substrate | ||||
Sequence: RN | ||||||
Binding site | 257 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 280 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 282 | 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 > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Saccharibacillus
Accessions
- Primary accessionA0A4Y6UT54
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MAKKVCVLVAGSWGTALA | ||||||
Chain | PRO_5038742980 | 19-346 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | |||
Sequence: MVLADNGHDVRLWARSEEHVQEINETRENSRFLPGVKLPDGLRATSDMQDALSEAEAVIIASPSKAMREVARALKPFWNEDMLCVHATKGMETGTLKRMSTIIAEELGCEESKIGVICGPSHAEEVARRRPTTIVVASANEGEAQRAQNLLMNAYFRVYTNRDVLGAELAGAFKNIIALGAGMSDGLEYGDNAKAALLTRGLAEITRIGTEMGANPLTFSGLAGVGDLVVTATSKHSRNWRAGYMIGQGKPLQEVLDSMGMVVEGIRTTEAAHFISQKYKVQMPIAEQLYRVLFEDLDPKTAVEALMGRGPKTEMEMISQETWEQWHT |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-160 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: KVCVLVAGSWGTALAMVLADNGHDVRLWARSEEHVQEINETRENSRFLPGVKLPDGLRATSDMQDALSEAEAVIIASPSKAMREVARALKPFWNEDMLCVHATKGMETGTLKRMSTIIAEELGCEESKIGVICGPSHAEEVARRRPTTIVVASANEG | ||||||
Domain | 181-322 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DVLGAELAGAFKNIIALGAGMSDGLEYGDNAKAALLTRGLAEITRIGTEMGANPLTFSGLAGVGDLVVTATSKHSRNWRAGYMIGQGKPLQEVLDSMGMVVEGIRTTEAAHFISQKYKVQMPIAEQLYRVLFEDLDPKTAVE |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length346
- Mass (Da)37,767
- Last updated2019-09-18 v1
- Checksum67EA74FF2C49259C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP041217 EMBL· GenBank· DDBJ | QDH19517.1 EMBL· GenBank· DDBJ | Genomic DNA |