A0A0X8I8F2 · A0A0X8I8F2_9CREN

  • Protein
    Glycerol-1-phosphate dehydrogenase [NAD(P)+]
  • Gene
    egsA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site97-101NAD+ (UniProtKB | ChEBI)
Binding site119-122NAD+ (UniProtKB | ChEBI)
Binding site124glycerol (UniProtKB | ChEBI)
Binding site124substrate
Binding site128NAD+ (UniProtKB | ChEBI)
Binding site171Zn2+ (UniProtKB | ChEBI); catalytic
Binding site171glycerol (UniProtKB | ChEBI)
Binding site171substrate
Binding site251Zn2+ (UniProtKB | ChEBI); catalytic
Binding site251glycerol (UniProtKB | ChEBI)
Binding site255substrate
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267glycerol (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglycerol-1-phosphate dehydrogenase (NAD+) activity
Molecular Functionglycerol-1-phosphate dehydrogenase (NADP+) activity
Molecular Functionmetal ion binding
Biological Processglycerophospholipid metabolic process
Biological Processphospholipid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycerol-1-phosphate dehydrogenase [NAD(P)+]
  • EC number
  • Short names
    G1P dehydrogenase
    ; G1PDH
  • Alternative names
    • Enantiomeric glycerophosphate synthase
    • sn-glycerol-1-phosphate dehydrogenase

Gene names

    • Name
      egsA
    • ORF names
      SE86_02375

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 7A
  • Taxonomic lineage
    Archaea > Thermoproteota > Thermoprotei > Acidilobales > Acidilobaceae > Acidilobus

Accessions

  • Primary accession
    A0A0X8I8F2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the glycerol-1-phosphate dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    351
  • Mass (Da)
    37,404
  • Last updated
    2016-04-13 v1
  • MD5 Checksum
    361975CB668858A43BE6A20C32825BC1
MEQHVIELPKRVVVGDGVLKSIGAHMKEMFKGGSAVLVVTGPHVLNTLYNEVKELLEDSGFSVSYTLAGPATVEEAVRLAEEASREKVDVLLGLGGGRSIDLAKYAAAESGKEFVSVPTAPSHDGITSPFATLHGFERPYSKLAKPPKLLLLDIDVISSAPRRLASAGFGDLIGKYTAVLDWKLAHNLRGEYYGAYAASLALMSAKHVSAYAKKIGLGSKDGVRALVEALVSSGVAMCIAGSSRPASGSEHLFAHALETISESPPLHGEAVGVGTILMSYLYGMRWKEIRRLLKEAGAPVNAKELGVNNDEVIEALVRAASIRPERYTILGERGLTREAAEELATKTMVIE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010515
EMBL· GenBank· DDBJ
AMD30416.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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