A0AAD1LXC9 · A0AAD1LXC9_9PSED

  • Protein
    Glycerol-3-phosphate dehydrogenase [NAD(P)+]
  • Gene
    gpsA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site47-52NAD+ (UniProtKB | ChEBI)
Binding site50NADPH (UniProtKB | ChEBI)
Binding site51NADPH (UniProtKB | ChEBI)
Binding site71NADPH (UniProtKB | ChEBI)
Binding site88NADPH (UniProtKB | ChEBI)
Binding site144NADPH (UniProtKB | ChEBI)
Binding site144sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site144substrate
Binding site172sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site176NAD+ (UniProtKB | ChEBI)
Binding site176NADPH (UniProtKB | ChEBI)
Active site227Proton acceptor
Binding site227sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site280sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site290sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site291NAD+ (UniProtKB | ChEBI)
Binding site291NADPH (UniProtKB | ChEBI)
Binding site291sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site291-292substrate
Binding site292sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site315NADPH (UniProtKB | ChEBI)
Binding site317NADPH (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
Molecular FunctionNAD binding
Biological Processcarbohydrate metabolic process
Biological Processglycerol-3-phosphate biosynthetic process
Biological Processglycerol-3-phosphate catabolic process
Biological Processglycerophospholipid metabolic process
Biological Processphospholipid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycerol-3-phosphate dehydrogenase [NAD(P)+]
  • EC number
  • Alternative names
    • NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase
    • NAD(P)H-dependent dihydroxyacetone-phosphate reductase

Gene names

    • Name
      gpsA
    • ORF names
      PHLH3_43920

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • St386
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0AAD1LXC9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_504206799920-377Glycerol-3-phosphate dehydrogenase [NAD(P)+]

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-196Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal
Domain216-357Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    377
  • Mass (Da)
    40,377
  • Last updated
    2024-05-29 v1
  • Checksum
    392B8EE206473E17
MVSFLQLVVIVAGAGRALAAPYNAPHCHLVWMNGLHMTEQRPIAVLGGGSFGTAVANLLAENGHPVRQWMRDPEQAEAIRVNRENPRYLKGIKIRPEVEPVTDLQATLEGSDLFFVALPSSALRSVLAPYAERLSGKLLVSLTKGIEAKTFKLMSEILEEIAPKARIGVISGPNLAREIAEHALTATVVASEDEELCQRVQAALHGRTFRVYASADRFGVELGGALKNVYAIIAGMAVALGMGENTKSMLITRALAEMTRFAVSQGANPMTFLGLAGVGDLIVTCSSPKSRNYQVGFALGQGLSLDEAVSRLGEVAEGVNTLKVLKAKSQEAGVYMPLVAGLHAILFEGRTLEQVIELLMRGEPKTDVDFISTSGFN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP021900
EMBL· GenBank· DDBJ
BBP54766.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp