G6Y6U9 · G6Y6U9_9HYPH
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids336 (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 | 18-23 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGAWG | ||||||
Binding site | 22 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 42 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 58 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 115 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 115 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 115 | substrate | ||||
Sequence: K | ||||||
Binding site | 143 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 145 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 147 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 147 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 198 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 198 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 251 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 261 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 262 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 262 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 262 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 262-263 | substrate | ||||
Sequence: RN | ||||||
Binding site | 263 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 281 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 283 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
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 > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Mesorhizobium
Accessions
- Primary accessionG6Y6U9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 12-31 | Helical | ||||
Sequence: WRVAVLGGGAWGTALALAML |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-167 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: VAVLGGGAWGTALALAMLRAGHFVRLYARDPETVAAIDHGENPRYLPGIAIEPGIVATSDIRAALDGADCVLAVAPAQALRSMLAAAKDHVPKSIPLVLCAKGIERDTGALLSTIVENILPENPVAALSGPSFATDVARGLPTAVVVAARDADL | ||||||
Domain | 187-322 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DLVGVEIGGALKNVFAIAAGAVTGAKLGASAQAAMVTRGFVELRRIGAAFGARPETLMGLSGLGDLLLTCSSAQSRNFAYGLALGQGKPLAGLPLAEGVPTAAIAARIAIERQIDAPIITAIAAILEGTVTVRQAV |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)34,213
- Last updated2012-01-25 v1
- Checksum689FF671B152142F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGSN01000078 EMBL· GenBank· DDBJ | EHH12509.1 EMBL· GenBank· DDBJ | Genomic DNA |