A0A2N3REV3 · A0A2N3REV3_9XANT
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids341 (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: GAGSWG | ||||||
Binding site | 15 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 16 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 36 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 53 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 110 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 110 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 110 | substrate | ||||
Sequence: K | ||||||
Binding site | 139 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 141 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 143 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 143 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 194 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 194 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 247 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 257 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 258 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 258 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 258 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 258-259 | substrate | ||||
Sequence: RN | ||||||
Binding site | 259 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 282 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 284 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Xanthomonas
Accessions
- Primary accessionA0A2N3REV3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-163 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: KIAVLGAGSWGTALAALLARHGYSTVLWGRDAAMVDIIDRTHENARYLPGIPLPDSLRATTDLQAAVADATWILVVVPSHAFTETIRLIAPLRPADAGVAWATKGFEPGSGRFLHEVARDILGPSVPLAVVTGPSFAKEVTLGLPTAVTVHGDDATF | ||||||
Domain | 183-321 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DMVGAELGGAMKNVLAVATGVADGMQLGLNARAGLITRGLNEMLRLAAAIGARPETLMGLAGLGDLVLTCTGDLSRNRRLGLALGRGQSLNDAIREIGQVVESVQTADEVMRQAEHHGIELPISNAVRAVLHGEITPEA |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length341
- Mass (Da)35,858
- Last updated2018-04-25 v1
- Checksum096E0E778F595685