P72010 · G1PDH_METTH

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. Is also able to catalyze the reverse reaction, i.e. the NAD(P)+-dependent oxidation of G1P but not of G3P. Is not active toward glycerol, dihydroxyacetone, glyceraldehyde-3-phosphate, glyceraldehyde and glycerol-2-phosphate.

Miscellaneous

G1PDH is a pro-R type dehydrogenase, which selectively transfers the pro-R hydrogen from NADH to dihydroxyacetonephosphate.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Activity regulation

Partially inhibited by divalent metal cations such as Co2+, Cu2+ and Ni2+.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.17 mMDHAPin the presence of NADH as coenzyme
0.58 mMDHAPin the presence of NADPH as coenzyme
0.129 mMNADH
0.025 mMNADPH
16.3 mMG1Pin the presence of NAD as coenzyme
4.8 mMG1Pin the presence of NADP as coenzyme
0.127 mMNAD+
0.27 mMNADP+
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
610 μmol/min/mgfor DHAP reduction with NADH as co
303 μmol/min/mgfor DHAP reduction with NADPH as co
39.8 μmol/min/mgfor G1P oxidation with NADH as co
23.9 μmol/min/mgfor G1P oxidation with NADPH as co

pH Dependence

Optimum pH is 6.6-7-4. Activity decreases gradually at pH over 7.4 or below 6.6.

Temperature Dependence

Optimum temperature is 75 degrees Celsius.

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site94-98NAD+ (UniProtKB | ChEBI)
Binding site116-119NAD+ (UniProtKB | ChEBI)
Binding site121substrate
Binding site125NAD+ (UniProtKB | ChEBI)
Binding site168substrate
Binding site168Zn2+ (UniProtKB | ChEBI); catalytic
Binding site248Zn2+ (UniProtKB | ChEBI); catalytic
Binding site252substrate
Binding site264Zn2+ (UniProtKB | ChEBI); catalytic

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
    • Ordered locus names
      MTH_610

Organism names

Accessions

  • Primary accession
    P72010

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001573451-347Glycerol-1-phosphate dehydrogenase [NAD(P)+]

Proteomic databases

Interaction

Subunit

Homooctamer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    347
  • Mass (Da)
    36,963
  • Last updated
    1997-02-01 v1
  • Checksum
    46D3600C30515413
MDPRKIQLPREIYTGPGVIEDTGRICRDLRFEGRAMVVTGPRTLQIAGEAAIESLQAEGFEVDQVTVDDATMASVRNVQDGLDGVSVVLGVGGGKVIDVAKMSATLEGLHFISVPTAASHDGIASPRASIRNGEGTASLEASSPIGVIADTEIISRAPFRLLASGCADIISNYTAIMDWKLAHRLLNERYSESAAALSLMTAKMIIKSADAIKEGLEESARLAVKSLISSGIAISIAGSSRPASGSEHKFSHALDMIAPKPALHGEQCGVGTIMMMHLHGGDWQFIRDALARINAPTTAAELGIDPEYIIEALTMAHNIRRERYTILGDRGLTREAAERLAKITEVI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D88555
EMBL· GenBank· DDBJ
BAA13644.1
EMBL· GenBank· DDBJ
Genomic DNA
AE000666
EMBL· GenBank· DDBJ
AAB85116.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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