A0A120I024 · A0A120I024_9MICO

  • 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.

Type
IDPosition(s)Description
Binding site24-29NAD+ (UniProtKB | ChEBI)
Binding site27NADPH (UniProtKB | ChEBI)
Binding site28NADPH (UniProtKB | ChEBI)
Binding site48NADPH (UniProtKB | ChEBI)
Binding site49NADPH (UniProtKB | ChEBI)
Binding site65NADPH (UniProtKB | ChEBI)
Binding site122NADPH (UniProtKB | ChEBI)
Binding site122sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site122substrate
Binding site152sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site156NAD+ (UniProtKB | ChEBI)
Binding site156NADPH (UniProtKB | ChEBI)
Active site207Proton acceptor
Binding site207sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site260sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site270sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site271NAD+ (UniProtKB | ChEBI)
Binding site271NADPH (UniProtKB | ChEBI)
Binding site271sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site271-272substrate
Binding site272sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site297NADPH (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
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
      AWU67_03995

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ERGS5:02
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Microterricola

Accessions

  • Primary accession
    A0A120I024

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain20-176Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal
Domain196-335Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal
Region333-359Disordered
Compositional bias347-356Basic and acidic residues

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    40,403
  • Last updated
    2016-04-13 v1
  • MD5 Checksum
    6CB2FAE01B70BB0FE49277992BE85375
MTPRAPKNPKTPTIKPGTRVAVLGAGSWGTTFAKILADGGADVVLWARRPELAREIQEAKRNSDYLPGINLPISLRATSRLDLALAGAEQVFVSVPSQSLRENLITAEPHIGANAIIVSLMKGVERSTGLRMSEVIEQVLPISTDRIAAISGPNLALEIAKEQPTAAVVSSTSLETAQAVALLARNGYFRTFVNTDVIGTEFGGVLKNLIAVAIGIVDGVGYGENTKASIITRGLVEMTDFAVAYGAHPETLSGLAGLGDLIATCQSPLSRNNTAGRLLGQGYSQADVVKQMQQTTEGLASVSPILELAKAKGVEMPIVEQVRQVLAGTLNPRDIAPHLTTDSDEPQGERTLDDAQAHGSAAVWGSVKRAFDQLRHGGRGPLGD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias347-356Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP014145
EMBL· GenBank· DDBJ
AMB58157.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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