A0A2P6MKI6 · A0A2P6MKI6_ALKUR

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site8-13NAD+ (UniProtKB | ChEBI)
Binding site11NADPH (UniProtKB | ChEBI)
Binding site12NADPH (UniProtKB | ChEBI)
Binding site32NADPH (UniProtKB | ChEBI)
Binding site49NADPH (UniProtKB | ChEBI)
Binding site106NADPH (UniProtKB | ChEBI)
Binding site106sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site106substrate
Binding site134sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site136sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site138NAD+ (UniProtKB | ChEBI)
Binding site138NADPH (UniProtKB | ChEBI)
Active site189Proton acceptor
Binding site189sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site242sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site252sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site253NAD+ (UniProtKB | ChEBI)
Binding site253NADPH (UniProtKB | ChEBI)
Binding site253sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site253-254substrate
Binding site254sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site277NADPH (UniProtKB | ChEBI)
Binding site279NADPH (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionglycerol-3-phosphate dehydrogenase (NADP+) activity
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
      C6I21_02440

Organism names

Accessions

  • Primary accession
    A0A2P6MKI6

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain5-158Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal
Domain178-319Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal
Region330-349Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    349
  • Mass (Da)
    37,694
  • Last updated
    2018-05-23 v1
  • Checksum
    7C74BC320BE00565
MKQTAVIGAGSWGTALALVLADNGLEVDLWARSEKQAEAMHSSRRNMRYLPGVELPEQIKPTASLETAVKDKDMIVLVVPTKAVREVLPALRPLLKEGAVIAHASKGIEPETHLRVSEVIAEELPGHPVACLSGPSHAEEVCKRQPTTVTSSSLHMETAELVQDVFMNTYFRVYTNPDLTGVEIGGSLKNIIAIGSGMTSGLGFGDNARAALMTRGLAEISRLGVKLGADPLTFSGLSGLGDLIVTCTSYHSRNWRAGNMIGKGMTINQVETEMGMVVEGVRTTKAAQQLAEKLDVEMPITSELYAVLFENKDVEEAVEALMGRVKKHEMEAPAVSRNTNRDPLDHFEP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PVNS01000002
EMBL· GenBank· DDBJ
PRO66800.1
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.
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