A0A2S6CP70 · A0A2S6CP70_9CYAN
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids325 (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+ + NADH
Pathway
Membrane lipid metabolism; glycerophospholipid metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12-17 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAWG | ||||||
Binding site | 16 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 36 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 37 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 86 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 86 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 86 | substrate | ||||
Sequence: K | ||||||
Binding site | 114 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 118 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 169 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 169 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 222 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 232 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 233 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 233 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 233 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 233-234 | substrate | ||||
Sequence: RN | ||||||
Binding site | 234 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 259 | 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
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Aphanizomenonaceae > Cuspidothrix
Accessions
- Primary accessionA0A2S6CP70
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-37 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: NITILGAGAWGQALAHLAAINQHTVRLWSRH | ||||||
Domain | 41-136 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: SLEDTLANTDIILCAISMKGVRDVANLVNSVNEKSLKNTIVVTATKGLEPYTTYTPSQIWETIFPHQPVVVLSGPNLSKEIEQKLPAATVVASKNV | ||||||
Domain | 158-298 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DPVGVELGGTLKNVIAISAGVCDGLHLGTNAKAALVTRGLTEMVRIGNTLGAKTETFYGLSGLGDLLATCNSPLSRNYQVGYQLANSKTLPEVLSSLSGTAEGVNTCRVLMEIAQKHSIAIPITEQVYQLLAGEITPRQAL |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length325
- Mass (Da)35,086
- Last updated2018-07-18 v1
- Checksum0169DEF2A8615657
Keywords
- Technical term