A0A365PS77 · A0A365PS77_9GAMM
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids340 (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
- 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 | 11-16 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGSFG | ||||||
Binding site | 14 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 15 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 35 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 52 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 108 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 108 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 108 | substrate | ||||
Sequence: K | ||||||
Binding site | 136 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 140 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 140 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 191 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 191 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 244 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 254 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 255 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 255 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 255 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 255-256 | substrate | ||||
Sequence: RN | ||||||
Binding site | 256 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 279 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 281 | 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 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 > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Stutzerimonas
Accessions
- Primary accessionA0A365PS77
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-160 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: IAVLGGGSFGTAIANLLAENGHSVRLWMRDAEQAESIRTHRQNPRYLKGVTLLPGVCPVTDLGQTLAECQLIFVALPSSALRQALSPFADHLSGKMLVSTTKGIEAQGFMLMSQILEEIAPQARIGVISGPNLAREVAEHALTATVVASDDEAL | ||||||
Domain | 180-320 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DRFGVELGGALKNVYAIMAGMAAALGMGENTRSMLITRALAEMTRFAVRLGANPMTFLGLAGVGDLIVTCTSTKSRNFQVGHALGEGLSLDEAVSRLGEVAEGVNTIKVLKTKAEELQVYMPLVAGLHAILYEGRTLDQVI |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length340
- Mass (Da)36,282
- Last updated2018-11-07 v1
- ChecksumD90B5EE66FF45548