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UniProt functional annotation for P0A9B2 | ||
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| UniProt code: P0A9B2. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| 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:0000269|PubMed:2659073}. |
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| 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:0000269|PubMed:2659073}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=15 uM for BPG {ECO:0000269|PubMed:2659073}; KM=42 uM for NAD {ECO:0000269|PubMed:2659073}; KM=1500 uM for G3P {ECO:0000269|PubMed:2659073}; Note=Kcat is 1056 sec(-1) for dehydrogenase activity.; |
| Pathway: | |
Carbohydrate degradation; glycolysis; pyruvate from D- glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984}. |
| Subcellular location: | |
Cytoplasm {ECO:0000305}. |
| Similarity: | |
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.