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UniProt functional annotation for P00934 | ||
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| UniProt code: P00934. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction. {ECO:0000269|PubMed:7907888}. |
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| Catalytic activity: | |
Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate; Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1; Evidence={ECO:0000269|PubMed:7907888}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:7907888}; |
| Activity regulation: | |
Is competitively inhibited by L-threo-3- hydroxyhomoserine phosphate. {ECO:0000269|PubMed:7907888}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.5 mM for O-phospho-L-homoserine {ECO:0000269|PubMed:7907888}; Vmax=9.3 umol/min/mg enzyme {ECO:0000269|PubMed:7907888}; |
| Pathway: | |
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5. |
| Similarity: | |
Belongs to the threonine synthase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.