A8AUM5 · GPDA_STRGC
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids338 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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+ + NADHThis reaction proceeds in the backward direction.
Pathway
Membrane lipid metabolism; glycerophospholipid metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 14 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 108 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 108 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 139 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 141 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 143 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 194 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 194 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 247 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 257 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 258 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 258 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 259 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 282 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 284 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionA8AUM5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000080323 | 1-338 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | |||
Sequence: MDKQRVAVIGPGSWGTALSQVLNDNGHEVRIWGNIAEQIDEINQAHTNTRYFKDTVLDEKIKAYHSLAEALDGADAVLFVVPTKVTRLVAKQVAQILDHNVKVMHASKGLEPDSHERISTILEEEIPSELRSEIVVVSGPSHAEETIVRDITLITAASKDLEAAKYVQKLFSNHYFRLYTNTDVVGVETAGALKNIIAVGAGALHGLGYGDNAKAAIITRGLAEITRLGVKLGASPLTYSGLSGVGDLIVTGTSIHSRNWRAGDALGRGEKLADIEANMGMVIEGISTTKAAYELAQELDVYMPITQAIYKVIYQGHDIKEAIFEIMNNEFKAENEWS |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)36,777
- Last updated2007-10-23 v1
- ChecksumCAE8AE7EC6E4910C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000725 EMBL· GenBank· DDBJ | ABV10937.1 EMBL· GenBank· DDBJ | Genomic DNA |