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V8CCH0 · V8CCH0_9HELI

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.

Type
IDPosition(s)Description
Binding site46-51NAD+ (UniProtKB | ChEBI)
Binding site50NADPH (UniProtKB | ChEBI)
Binding site69NADPH (UniProtKB | ChEBI)
Binding site70NADPH (UniProtKB | ChEBI)
Binding site127NADPH (UniProtKB | ChEBI)
Binding site127sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site127substrate
Binding site155sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site157sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site159NAD+ (UniProtKB | ChEBI)
Binding site159NADPH (UniProtKB | ChEBI)
Active site209Proton acceptor
Binding site209sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site262sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site272sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site273NAD+ (UniProtKB | ChEBI)
Binding site273NADPH (UniProtKB | ChEBI)
Binding site273sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site273-274substrate
Binding site274sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site297NADPH (UniProtKB | ChEBI)
Binding site299NADPH (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
      HMPREF2086_00374

Organism names

  • Taxonomic identifier
  • Strain
    • MIT 99-5501
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    V8CCH0

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-24Disordered
Compositional bias7-21Polar residues
Domain84-179Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal
Domain198-332Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    343
  • Mass (Da)
    36,497
  • Last updated
    2014-02-19 v1
  • MD5 Checksum
    4B5D34BC90F953B5DF16B7AC3ED93447
MPPKKSTKSTPAESSAKSNLQDCQKDTREDIAHTSLHSPAQVSVCGGGAWGSALAYALSHSTDVHIASRRTLALPSDTPCQILQVDCASALSSHFVIIAISTPNLRKWLSLQSKFLQPSTKYLFASKGIEEGSGAFVHTIALDFIPKENLAFLSGPSFAAEVRAKLPCALAIHAYNDEVAKDFAKFFPSFIKPYTGGDVIGAEVSGAYKNVLAIAGGICDELKLGHNAKAALLARGLIEMERFGRYFGGESKTFLGLEGAGDLFLSANSTLSRNYRVGVGLAQGKDIDSILCELGEVAEGVRTAYAIQGIAKKHDIYTPIVNEVVGILQGKSCKEGILSLMSR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias7-21Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AZJI01000001
EMBL· GenBank· DDBJ
ETD25039.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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