A0A0I9TTF5 · A0A0I9TTF5_9MYCO
- ProteinGlycerol-3-phosphate dehydrogenase [NAD(P)+]
- GenegpsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids342 (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 | 15-20 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGSWG | ||||||
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 | 113 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 113 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 113 | substrate | ||||
Sequence: K | ||||||
Binding site | 141 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 145 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 145 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Active site | 196 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 196 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 249 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 259 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 260 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260-261 | substrate | ||||
Sequence: RN | ||||||
Binding site | 261 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 284 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 286 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acyltransferase activity | |
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 > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionA0A0I9TTF5
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-165 | Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal | ||||
Sequence: KVVVFGGGSWGTTVASICARRGPTLQWVRSEVTAKDINEQHRNSRYLGNDVVLSDTLRATTDFAEAARCADVVVMGVPSHGFRGVLTELAKELRPWVPVVSLVKGLEQGTNMRMSQIVEEVLPGHPAGILAGPNIAREVAEGYAAAAVLAMPDQHL | ||||||
Domain | 185-325 | Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal | ||||
Sequence: DVIGVEVAGALKNVFAIAVGMGYSLGIGENTRALVIARALREMTKLGVALGGRSETFPGLAGLGDLIVTCTSQRSRNRHVGEQLGAGKPIDEIIASMNQVAEGVKAASVVMEFATEFGLSMPIAREVDAVINHASTVEQAY |
Sequence similarities
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length342
- Mass (Da)36,362
- Last updated2015-10-14 v1
- ChecksumA0206E8F76B8E83F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LDPR01000003 EMBL· GenBank· DDBJ | KLO38001.1 EMBL· GenBank· DDBJ | Genomic DNA |