A0A2W5MVP0 · A0A2W5MVP0_9BACT

  • 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.
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 site8-13NAD+ (UniProtKB | ChEBI)
Binding site12NADPH (UniProtKB | ChEBI)
Binding site32NADPH (UniProtKB | ChEBI)
Binding site49NADPH (UniProtKB | ChEBI)
Binding site82NAD+ (UniProtKB | ChEBI)
Binding site105NADPH (UniProtKB | ChEBI)
Binding site105sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site105substrate
Binding site133sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site135sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site137NAD+ (UniProtKB | ChEBI)
Binding site137NADPH (UniProtKB | ChEBI)
Active site188Proton acceptor
Binding site188sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site241sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site251sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site252NAD+ (UniProtKB | ChEBI)
Binding site252NADPH (UniProtKB | ChEBI)
Binding site252sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site252-253substrate
Binding site253sn-glycerol 3-phosphate (UniProtKB | ChEBI)
Binding site276NADPH (UniProtKB | ChEBI)
Binding site278NADPH (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionacyltransferase activity
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
      DI551_07880

Organism names

  • Taxonomic identifier
  • Strain
    • S2_005_002_R2_29
  • Taxonomic lineage
    Bacteria > Bdellovibrionota > Bdellovibrionia > Bdellovibrionales > Pseudobdellovibrionaceae > Micavibrio

Accessions

  • Primary accession
    A0A2W5MVP0

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-156Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal
Domain177-317Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    330
  • Mass (Da)
    34,582
  • Last updated
    2018-09-12 v1
  • Checksum
    203261C6A8878698
MDTIGIIGGGAWGTALAQSLAQTGKHVVIWAREEDLVTSINNKHENISYLPGVTLHENITATGSLSVAARAEALLIVTPAQFLRTTLQSLKPDLRPDQPLVICAKGVEIESGMLLSQIAQEIVPESPIAILTGPTFAAEIARGLPSAVTLAMKDKGVAEKLAEDLSSRSLRMYASDDIIGAQVGGAVKNVIAIACGIIEGKKLGDSARAALVTRGLAEIARLATALGAKKETLMGMCGVGDMILTCSSMQSRNFSLGVALGQGKTLQEILAQRNSVTEGVYTAKALVTMAKNNAVEMPVSEAVHKCLTEGADVDDIIVKMLDRPTRSEVA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QFQB01000056
EMBL· GenBank· DDBJ
PZQ45256.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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