UniProt functional annotation for Q9RME2

UniProt code: Q9RME2.

Organism: Alkalihalobacillus alcalophilus (Bacillus alcalophilus).
Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
 
Function: Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000269|PubMed:14646107}.
 
Catalytic activity: Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810, ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
Catalytic activity: Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2- oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452, ChEBI:CHEBI:58538; EC=2.6.1.52;
Cofactor: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:15608117, ECO:0000269|PubMed:15883191}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:15608117, ECO:0000269|PubMed:15883191};
Biophysicochemical properties: pH dependence: Optimum pH is 9.0. At pH 9.5, retains more than 60% of its maximum activity. At pH 7.0 the relative activity is less than 10%. {ECO:0000269|PubMed:15608117};
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Subunit: Homodimer. {ECO:0000269|PubMed:14646107, ECO:0000269|PubMed:15608117, ECO:0000269|PubMed:15883191}.
Subcellular location: Cytoplasm {ECO:0000250}.
Similarity: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.