A0AAD1LXC9 · A0AAD1LXC9_9PSED
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids377 (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 | 47-52 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGSFG | ||||||
Binding site | 50 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 51 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 71 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 88 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 144 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 144 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 144 | substrate | ||||
Sequence: K | ||||||
Binding site | 172 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 176 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 176 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 227 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 227 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 280 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 290 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 291 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 291 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 291 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 291-292 | substrate | ||||
Sequence: RN | ||||||
Binding site | 292 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 315 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 317 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0AAD1LXC9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MVSFLQLVVIVAGAGRALA | ||||||
Chain | PRO_5042067999 | 20-377 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | |||
Sequence: APYNAPHCHLVWMNGLHMTEQRPIAVLGGGSFGTAVANLLAENGHPVRQWMRDPEQAEAIRVNRENPRYLKGIKIRPEVEPVTDLQATLEGSDLFFVALPSSALRSVLAPYAERLSGKLLVSLTKGIEAKTFKLMSEILEEIAPKARIGVISGPNLAREIAEHALTATVVASEDEELCQRVQAALHGRTFRVYASADRFGVELGGALKNVYAIIAGMAVALGMGENTKSMLITRALAEMTRFAVSQGANPMTFLGLAGVGDLIVTCSSPKSRNYQVGFALGQGLSLDEAVSRLGEVAEGVNTLKVLKAKSQEAGVYMPLVAGLHAILFEGRTLEQVIELLMRGEPKTDVDFISTSGFN |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-196 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: IAVLGGGSFGTAVANLLAENGHPVRQWMRDPEQAEAIRVNRENPRYLKGIKIRPEVEPVTDLQATLEGSDLFFVALPSSALRSVLAPYAERLSGKLLVSLTKGIEAKTFKLMSEILEEIAPKARIGVISGPNLAREIAEHALTATVVASEDEEL | ||||||
Domain | 216-357 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DRFGVELGGALKNVYAIIAGMAVALGMGENTKSMLITRALAEMTRFAVSQGANPMTFLGLAGVGDLIVTCSSPKSRNYQVGFALGQGLSLDEAVSRLGEVAEGVNTLKVLKAKSQEAGVYMPLVAGLHAILFEGRTLEQVIE |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)40,377
- Last updated2024-05-29 v1
- Checksum392B8EE206473E17