Q6V0I0 · Q6V0I0_STAAU

  • Protein
    Glyceraldehyde-3-phosphate dehydrogenase
  • Gene
    gapC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.

Catalytic activity

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site12-13NAD+ (UniProtKB | ChEBI)
Binding site34NAD+ (UniProtKB | ChEBI)
Binding site120NAD+ (UniProtKB | ChEBI)
Binding site150-152D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Active site151Nucleophile
Site178Activates thiol group during catalysis
Binding site181D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site211-212D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site234D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site316NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Molecular FunctionNAD binding
Molecular FunctionNADP binding
Biological Processglucose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glyceraldehyde-3-phosphate dehydrogenase
  • EC number

Gene names

    • Name
      gapC

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BM10
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    Q6V0I0

Subcellular Location

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-151Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    36,250
  • Last updated
    2004-07-05 v1
  • Checksum
    96A7DFA936BDD294
MAVKVAINGFGRIGRLAFRRIQEVEGLEVVAVNDLTDDDMLAHLLKYDTMQGRFTGEVEVVDGGFRVNGKEVKSFSEPDASKLPWKDLNIDVVLECTGFYTDKDKAQAHIEAGAKKVLISAPATGDLKTIVFNTNHQELDGSETVVSGASCTTNSLAPVAKVLNDDFGLVEGLMTTIHAYTGDQNTQDAPHRKGDKRRARAAAENIIPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGSLTELTVVLEKPDVTVEQVNEAMKNASNESFGYTEDEIVSSDVVGMTYGSLFDATQTRVMSVGDRQLVKVAAWYDNEMSYTAQLVRTLAYLAELSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY356529
EMBL· GenBank· DDBJ
AAR13672.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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