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UniProt functional annotation for P19938 | ||
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| UniProt code: P19938. |
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| Organism: | |
Bacillus sp. (strain YM-1). |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. |
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| Function: | |
Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components. {ECO:0000269|PubMed:2914916, ECO:0000269|PubMed:9538014}. |
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| Catalytic activity: | |
Reaction=2-oxoglutarate + D-alanine = D-glutamate + pyruvate; Xref=Rhea:RHEA:15869, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810, ChEBI:CHEBI:29986, ChEBI:CHEBI:57416; EC=2.6.1.21; Evidence={ECO:0000269|PubMed:2914916, ECO:0000269|PubMed:9538014}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:7626635}; |
| Biophysicochemical properties: | |
Absorption: Abs(max)=279 nm {ECO:0000269|PubMed:2914916}; Note=Holoenzyme exhibits additional strong peaks at 333 nm and 415 nm. Addition of D-alanine causes a decrease in absorbance at 419 nm and an increase at 335 nm.; Kinetic parameters: KM=2.2 mM for D-alanine {ECO:0000269|PubMed:2914916}; KM=5.9 mM for alpha-ketoglutarate {ECO:0000269|PubMed:2914916}; KM=2.2 mM for alpha-ketobutyrate {ECO:0000269|PubMed:2914916}; KM=2.2 mM for alpha-ketovalerate {ECO:0000269|PubMed:2914916}; pH dependence: Optimum pH is 8.3. {ECO:0000269|PubMed:2914916}; Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:2914916}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:2914916, ECO:0000269|PubMed:7626635}. |
| Similarity: | |
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.