| IED ID | IndEnz0002005803 |
| Enzyme Type ID | protease005803 |
| Protein Name |
Glyceraldehyde-3-phosphate dehydrogenase GAPDH EC 1.2.1.12 NAD-dependent glyceraldehyde-3-phosphate dehydrogenase |
| Gene Name | gapA gap |
| Organism | Staphylococcus aureus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus |
| Enzyme Sequence | MAVKVAINGFGRIGRLAFRRIQEVEGLEVVAVNDLTDDDMLAHLLKYDTMQGRFTGEVEVVDGGFRVNGKEVKSFSEPDASKLPWKDLNIDVVLECTGFYTDKDKAQAHIEAGAKKVLISAPATGDLKTIVFNTNHQELDGSETVVSGASCTTNSLAPVAKVLNDDFGLVEGLMTTIHAYTGDQNTQDAPHRKGDKRRARAAAENIIPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGSLTELTVVLEKQDVTVEQVNEAMKNASNESFGYTEDEIVSSDVVGMTYGSLFDATQTRVMSVGDRQLVKVAAWYDNEMSYTAQLVRTLAYLAELSK |
| Enzyme Length | 336 |
| Uniprot Accession Number | P0A038 |
| Absorption | |
| Active Site | ACT_SITE 151; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q6GIL8 |
| Activity Regulation | |
| Binding Site | BINDING 34; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q6GIL8; BINDING 120; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q6GIL8; BINDING 181; /note=Glyceraldehyde 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q6GIL8; BINDING 198; /note=Glyceraldehyde 3-phosphate; /evidence=ECO:0000250|UniProtKB:P00362; BINDING 234; /note=Glyceraldehyde 3-phosphate; /evidence=ECO:0000250|UniProtKB:Q6GIL8; BINDING 316; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q6GIL8 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:Q6GIL8}; |
| DNA Binding | |
| EC Number | 1.2.1.12 |
| Enzyme 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. {ECO:0000250|UniProtKB:Q6GIL8}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. |
| nucleotide Binding | NP_BIND 12..13; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q6GIL8 |
| Features | Active site (1); Binding site (6); Chain (1); Nucleotide binding (1); Region (2); Site (1) |
| Keywords | Cytoplasm;Glycolysis;NAD;Nucleotide-binding;Oxidoreductase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,281 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:10300 |
| Cross Reference Brenda |