A0A9E0TA86 · A0A9E0TA86_UNCPS
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids329 (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 | 7-12 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGAWG | ||||||
Binding site | 11 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 32 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 49 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 104 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 104 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 104 | substrate | ||||
Sequence: K | ||||||
Binding site | 132 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 134 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 136 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 136 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 187 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 187 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 240 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 250 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 251 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 251 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 251 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 251-252 | substrate | ||||
Sequence: RN | ||||||
Binding site | 252 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 275 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 277 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
Accessions
- Primary accessionA0A9E0TA86
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MKIVVLGAGAWGTALAVSAAHA | ||||||
Chain | PRO_5038975764 | 23-329 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | |||
Sequence: SAHAVTLWARDAQQAATMQAARCNQRYLPGVAFPPALQVVAGDARALAAGAELVIIATPMAALRDMLQLLAGCQAPIAWLCKGFEAGTGLMAHEVCAQVAPQLASGVLSGPSFALEVARAQPTALVAASARERVREALVAAFHGHMLRVYASDDIVGVEVGGAVKNVLAIATGLCDGLQLGLNARAALITRGLAEMTRLGLALGARPDTFMGLSGLGDLVLTATGDLSRNRRVGLLLAGGQTLQQAVASLGHVAEGVYSARTVVQRARAAGVEMPIAECVVALLDGRLRAADAVALLMEREPTVERH |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-155 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: KIVVLGAGAWGTALAVSAAHASAHAVTLWARDAQQAATMQAARCNQRYLPGVAFPPALQVVAGDARALAAGAELVIIATPMAALRDMLQLLAGCQAPIAWLCKGFEAGTGLMAHEVCAQVAPQLASGVLSGPSFALEVARAQPTALVAASARER | ||||||
Domain | 176-316 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DIVGVEVGGAVKNVLAIATGLCDGLQLGLNARAALITRGLAEMTRLGLALGARPDTFMGLSGLGDLVLTATGDLSRNRRVGLLLAGGQTLQQAVASLGHVAEGVYSARTVVQRARAAGVEMPIAECVVALLDGRLRAADAV |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length329
- Mass (Da)33,763
- Last updated2023-05-03 v1
- Checksum0168030B91E31153