A0A218PXL4 · A0A218PXL4_9CYAN
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids311 (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 | 13-18 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAWG | ||||||
Binding site | 17 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 37 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 38 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 85 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 85 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 85 | substrate | ||||
Sequence: K | ||||||
Binding site | 113 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 117 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 168 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 168 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 221 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 231 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 232 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 232 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 232 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 232-233 | substrate | ||||
Sequence: RN | ||||||
Binding site | 233 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 258 | 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 > Cyanobacteriota > Cyanophyceae > Nostocales > Aphanizomenonaceae > Nodularia
Accessions
- Primary accessionA0A218PXL4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MIAVQKTTIAILGAGAWGLALA | ||||||
Chain | PRO_5013392912 | 23-311 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | |||
Sequence: DLASANGHQVRVWSRRGTANLAAVVQDAQIILSAISMKGVSDVVCQVKSCPLSPKTIFVTATKGLDPKTTCTPSQIWQTAFPHHPVVVLSGPNLSKEIQQSLPAATVAASNDTAAAELVQLVFSSPHFRVYTNPDPLGVELGGTLKNIMAIASGVCDGLHLGTNAKAALVTRGLTEIVRIGQSWGAKTETFYGLSGLGDLLATCNSPLSRNYQVGYQMAGGKTLTEILANLPGTAEGVNTCQVLVQRAKQHSIAIPITEQVYRLLEGEITPRQALSELMLRDTKAEYNC |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-38 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: IAILGAGAWGLALADLASANGHQVRVWSRR | ||||||
Domain | 40-137 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: TANLAAVVQDAQIILSAISMKGVSDVVCQVKSCPLSPKTIFVTATKGLDPKTTCTPSQIWQTAFPHHPVVVLSGPNLSKEIQQSLPAATVAASNDTAA | ||||||
Domain | 157-297 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DPLGVELGGTLKNIMAIASGVCDGLHLGTNAKAALVTRGLTEIVRIGQSWGAKTETFYGLSGLGDLLATCNSPLSRNYQVGYQMAGGKTLTEILANLPGTAEGVNTCQVLVQRAKQHSIAIPITEQVYRLLEGEITPRQAL |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length311
- Mass (Da)32,843
- Last updated2017-09-27 v1
- Checksum9A1C8940460F1B34