UniProt functional annotation for Q56232

UniProt code: Q56232.

Organism:		Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
Taxonomy:		Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
Function:		Catalyzes the reversible conversion of aspartate and 2- oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275). {ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:30771275, ECO:0000269|PubMed:8907187}.
Catalytic activity:		Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:8907187};
Catalytic activity:		Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate; Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934, ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78; Evidence={ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:30771275};
Cofactor:		Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11432784, ECO:0000269|PubMed:8907187};
Biophysicochemical properties:		Kinetic parameters: KM=1.1 mM for L-aspartate (at 45 degrees Celsius) {ECO:0000269|PubMed:8907187}; KM=1.0 mM for 2-oxoglutarate (at 45 degrees Celsius) {ECO:0000269|PubMed:8907187}; KM=150 uM for prephenate {ECO:0000269|PubMed:30771275}; KM=25.3 uM for oxaloacetate {ECO:0000269|PubMed:30771275}; Note=kcat is 7.7 sec(-1) toward prephenate. kcat is 32.2 sec(-1) toward oxaloacetate. {ECO:0000269|PubMed:30771275};
Subunit:		Homodimer. {ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784}.
Subcellular location:		Cytoplasm {ECO:0000305}.
Similarity:		Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.