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UniProt functional annotation for P0A9T0 | ||
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| UniProt code: P0A9T0. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000269|PubMed:8550422}. |
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| Catalytic activity: | |
Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:8550422}; |
| Catalytic activity: | |
Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.399; Evidence={ECO:0000269|PubMed:8550422}; |
| Activity regulation: | |
Displays feedback inhibition by L-serine. Inhibited by glycine. {ECO:0000269|PubMed:8550422}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=1.2 mM for 3-phospho-D-glycerate {ECO:0000269|PubMed:8550422}; KM=3.2 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:8550422}; KM=88 uM for 2-oxoglutarate {ECO:0000269|PubMed:8550422}; KM=0.37 mM for (R)-2-hydroxyglutarate {ECO:0000269|PubMed:8550422}; KM=2.9 mM for (S)-2-hydroxyglutarate {ECO:0000269|PubMed:8550422}; Vmax=183 nmol/min/mg enzyme for 3-phospho-D-glycerate oxidation {ECO:0000269|PubMed:8550422}; Vmax=9.27 umol/min/mg enzyme for 3-phosphonooxypyruvate reduction {ECO:0000269|PubMed:8550422}; Vmax=11.1 umol/min/mg enzyme for 2-oxoglutarate reduction {ECO:0000269|PubMed:8550422}; Vmax=237 nmol/min/mg enzyme for (R)-2-hydroxyglutarate oxidation {ECO:0000269|PubMed:8550422}; Vmax=83.3 nmol/min/mg enzyme for (S)-2-hydroxyglutarate oxidation {ECO:0000269|PubMed:8550422}; Note=kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2- hydroxyglutarate oxidation. kcat is 0.25 sec(-1) for (S)-2- hydroxyglutarate oxidation. {ECO:0000269|PubMed:8550422}; pH dependence: Optimum pH is 8.5 for the reductase activities and 9.0 for the dehydrogenase activities. {ECO:0000269|PubMed:8550422}; |
| Pathway: | |
Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. |
| Subunit: | |
Homotetramer. |
| Similarity: | |
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.