H0FCZ7 · H0FCZ7_9BURK
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids359 (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 | 15-20 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGSWG | ||||||
Binding site | 18 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 19 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 38 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 55 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 122 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 122 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 122 | substrate | ||||
Sequence: K | ||||||
Binding site | 150 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 152 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 154 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 154 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 205 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 205 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 258 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 268 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 269 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 269 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 269 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 269-270 | substrate | ||||
Sequence: RN | ||||||
Binding site | 270 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 294 | 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 > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Achromobacter
Accessions
- Primary accessionH0FCZ7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MNPPAPPRLRVAVLGAGSWGTALA | ||||||
Chain | PRO_5003533349 | 25-359 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | |||
Sequence: AAASRRHPTQLWARDAAQAASMAATHENARYLPGVSLPKNLQFSSDLDATLRCLQDDGGHRLIVLGVPVAGLTAICDELSRRLPALGLEDTPIVWTCKGFEADTARLPHEIMREALPGATGGALSGPSFAREVAQGLPVALTVASSSPALRDATTAAFHGAALRVYASTDLIGVEVGGALKNVIAVACGICDGLALGTNARAALITRGLAEMTRFGVALGAQAETFAGLTGLGDLVLTATGELSRNRRVGLEIGAGRKLADILASGITAEGVRCARAALERARAINVELPITEAVCAVLFDGVAPMTAVSALLARDARNEGADSGNPLQGPSGPA |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-172 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: VAVLGAGSWGTALAAAASRRHPTQLWARDAAQAASMAATHENARYLPGVSLPKNLQFSSDLDATLRCLQDDGGHRLIVLGVPVAGLTAICDELSRRLPALGLEDTPIVWTCKGFEADTARLPHEIMREALPGATGGALSGPSFAREVAQGLPVALTVASSSP | ||||||
Domain | 194-333 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DLIGVEVGGALKNVIAVACGICDGLALGTNARAALITRGLAEMTRFGVALGAQAETFAGLTGLGDLVLTATGELSRNRRVGLEIGAGRKLADILASGITAEGVRCARAALERARAINVELPITEAVCAVLFDGVAPMTAV |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)36,608
- Last updated2012-02-22 v1
- ChecksumB6FE4F684AA51779
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGUF01000074 EMBL· GenBank· DDBJ | EHK63790.1 EMBL· GenBank· DDBJ | Genomic DNA |