UniProt functional annotation for Q9I700

UniProt code: Q9I700.

Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
 
Function: Involved in the degradation of beta-alanine. Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L- alanine and 3-oxopropanoate. It can also accept both 4-aminobutyrate and (S)-alpha-methylbenzylamine (MBA) as amino-group donors in the presence of pyruvate as an amine acceptor. {ECO:0000269|PubMed:21622750, ECO:0000269|PubMed:23519665}.
 
Catalytic activity: Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18;
Cofactor: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:23519665, ECO:0000269|Ref.4};
Activity regulation: Inhibited by gabaculine (5-amino-1,3- cyclohexadienylcarboxylic acid). {ECO:0000269|PubMed:23519665}.
Subunit: Homotetramer. {ECO:0000269|PubMed:23519665, ECO:0000269|Ref.4}.
Induction: Activated by BauR. {ECO:0000269|PubMed:21622750}.
Disruption phenotype: Cells lacking this gene grow normally on putrescine, cadaverine, and GABA, but growth on beta-alanine is completely abolished. {ECO:0000269|PubMed:21622750}.
Similarity: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.